메뉴 건너뛰기




Volumn 1, Issue 2, 2005, Pages

Transfer RNA modification

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84924880646     PISSN: None     EISSN: 23246200     Source Type: Journal    
DOI: 10.1128/ecosalplus.4.6.2     Document Type: Article
Times cited : (11)

References (416)
  • 1
    • 0018079265 scopus 로고
    • Origin of the genetic code: a testable hypothesis based on tRNA structure, sequence, and kinetic proofreading
    • Hopfield JJ. 1978. Origin of the genetic code: a testable hypothesis based on tRNA structure, sequence, and kinetic proofreading. Proc Natl Acad Sci USA 75: 4334-4338.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4334-4338
    • Hopfield, J.J.1
  • 2
    • 0032554558 scopus 로고    scopus 로고
    • Reflections on the origin of the genetic code: a hypothesis
    • Di Giulio M. 1998. Reflections on the origin of the genetic code: a hypothesis. J Theor Biol 191: 191-196.
    • (1998) J Theor Biol , vol.191 , pp. 191-196
    • Di Giulio, M.1
  • 3
    • 84957846754 scopus 로고
    • The quantitative separation of purines, pyrimidines, and nucleosides by paper chromatography
    • Hotchkiss R. 1948. The quantitative separation of purines, pyrimidines, and nucleosides by paper chromatography. J Biol Chem 175: 315-332.
    • (1948) J Biol Chem , vol.175 , pp. 315-332
    • Hotchkiss, R.1
  • 4
    • 0345981608 scopus 로고
    • Nucleoside-5′-phosphates from ribonucleic acid
    • Cohn WE, Volkin E. 1951. Nucleoside-5′-phosphates from ribonucleic acid. Nature 167: 483-484.
    • (1951) Nature , vol.167 , pp. 483-484
    • Cohn, W.E.1    Volkin, E.2
  • 5
    • 0041794438 scopus 로고
    • Minor constituents of ribonucleic acids
    • Cohn WE. 1957. Minor constituents of ribonucleic acids. Fed Proc 16: 166.
    • (1957) Fed Proc , vol.16 , pp. 166
    • Cohn, W.E.1
  • 6
    • 0010728770 scopus 로고
    • 5-Ribosyl uracil, a carbon-carbon ribofuranosyl nucleoside in ribonucleic acids
    • Cohn WE. 1959. 5-Ribosyl uracil, a carbon-carbon ribofuranosyl nucleoside in ribonucleic acids. Biochim Biophys Acta 32: 570-571.
    • (1959) Biochim Biophys Acta , vol.32 , pp. 570-571
    • Cohn, W.E.1
  • 7
    • 0000661146 scopus 로고
    • Pseudouridine, a cabon-carbon linked ribonucleoside in ribonucleic acids: Isolation, structure, and chemical characteristics
    • Cohn WE. 1960. Pseudouridine, a cabon-carbon linked ribonucleoside in ribonucleic acids: Isolation, structure, and chemical characteristics. J Biol Chem 235: 1488-1498.
    • (1960) J Biol Chem , vol.235 , pp. 1488-1498
    • Cohn, W.E.1
  • 8
    • 0000568977 scopus 로고
    • Ribonucleic acids from yeast which contain a fifth nucleotide
    • Davis FF, Allen FW. 1957. Ribonucleic acids from yeast which contain a fifth nucleotide. J Biol Chem 227: 907-915.
    • (1957) J Biol Chem , vol.227 , pp. 907-915
    • Davis, F.F.1    Allen, F.W.2
  • 9
    • 49749161394 scopus 로고
    • Methylation studies on various uracil drivatives and on an isomer of uridine isolated from ribonucleic acid
    • Scannell JP, Crestfield AM, Allen FW. 1959. Methylation studies on various uracil drivatives and on an isomer of uridine isolated from ribonucleic acid. Biochim Biophys Acta 32: 406-412.
    • (1959) Biochim Biophys Acta , vol.32 , pp. 406-412
    • Scannell, J.P.1    Crestfield, A.M.2    Allen, F.W.3
  • 10
    • 0010687992 scopus 로고
    • Studies on an isomer of uridine isolated from ribonucleic acid
    • Yu C-T, Allen FW. 1959. Studies on an isomer of uridine isolated from ribonucleic acid. Biochim Biophys Acta 32: 393-406.
    • (1959) Biochim Biophys Acta , vol.32 , pp. 393-406
    • Yu, C.-T.1    Allen, F.W.2
  • 12
    • 0343647472 scopus 로고
    • Additional components in ribonucleic acid of rat-liver fractions
    • Dunn DB. 1959. Additional components in ribonucleic acid of rat-liver fractions. Biochim Biophys Acta 34: 286-288.
    • (1959) Biochim Biophys Acta , vol.34 , pp. 286-288
    • Dunn, D.B.1
  • 13
    • 25144499284 scopus 로고
    • The occurence of methylated guanines in ribonucleic acids from several sources
    • Smith JD, Dunn DB. 1959. The occurence of methylated guanines in ribonucleic acids from several sources. Biochem J 72: 294-300.
    • (1959) Biochem J , vol.72 , pp. 294-300
    • Smith, J.D.1    Dunn, D.B.2
  • 14
    • 0344437760 scopus 로고
    • Studies on microbial RNA I. Transfer of methyl groups from methionine to soluble RNA from Escherichia coli.
    • Svensson I, Boman HG, Eriksson KG, Kjellin K. 1963. Studies on microbial RNA. I. Transfer of methyl groups from methionine to soluble RNA from Escherichia coli. J Mol Biol 7: 254-271.
    • (1963) J Mol Biol , vol.7 , pp. 254-271
    • Svensson, I.1    Boman, H.G.2    Eriksson, K.G.3    Kjellin, K.4
  • 15
    • 0010742202 scopus 로고
    • A new enzyme of RNA synthesis: RNA methylase
    • Fleissner E, Borek E. 1962. A new enzyme of RNA synthesis: RNA methylase. Proc Natl Acad Sci USA 48: 1199-1203.
    • (1962) Proc Natl Acad Sci USA , vol.48 , pp. 1199-1203
    • Fleissner, E.1    Borek, E.2
  • 16
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese CR, Kandler O, Wheelis ML. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci USA 87: 4576-4579.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 18
    • 0001918945 scopus 로고    scopus 로고
    • Location and distribution of modified nucleotides in tRNA
    • Grosjean H and Benne R (ed), ASM Press, Washington, D.C
    • Auffinger P, Westhof E. 1998. Location and distribution of modified nucleotides in tRNA, p 569-576. In Grosjean H and Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 569-576
    • Auffinger, P.1    Westhof, E.2
  • 19
    • 0001494356 scopus 로고    scopus 로고
    • Appendix 1: Chemical structures and classification of posttranscriptionally modified nucleosides in RNA
    • Grosjean H and Benne R (ed), ASM Press, Washington, D.C
    • Motorin Y, Grosjean H. 1998. Appendix 1: Chemical structures and classification of posttranscriptionally modified nucleosides in RNA, p 543-549. In Grosjean H and Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 543-549
    • Motorin, Y.1    Grosjean, H.2
  • 20
    • 0002225492 scopus 로고
    • Transfer RNA modification in different organisms
    • Björk GR. 1986. Transfer RNA modification in different organisms. Chem Scr 26B:91-95.
    • (1986) Chem Scr , vol.26 B , pp. 91-95
    • Björk, G.R.1
  • 21
    • 0002596822 scopus 로고    scopus 로고
    • Modified nucleosides always were: an evolutionary model
    • Grosjean H and Benne R (ed), ASM Press, Washington, D.C
    • Cermakian N, Cedergren R. 1998. Modified nucleosides always were: an evolutionary model, p 535-541. In Grosjean H and Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 535-541
    • Cermakian, N.1    Cedergren, R.2
  • 22
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a tRNA Psi 55 pseudouridine synthase: Nucleotide flipping by an RNAmodifying enzyme
    • Hoang C, FerreDAmare AR. 2001. Cocrystal structure of a tRNA Psi 55 pseudouridine synthase: Nucleotide flipping by an RNAmodifying enzyme. Cell 107: 929-939.
    • (2001) Cell , vol.107 , pp. 929-939
    • Hoang, C.1    Ferre, D.2    Amare, A.R.3
  • 23
    • 0036242429 scopus 로고    scopus 로고
    • Chips off the old block
    • Mueller EG. 2002. Chips off the old block. Nat Struct Biol 9: 320-322.
    • (2002) Nat Struct Biol , vol.9 , pp. 320-322
    • Mueller, E.G.1
  • 26
    • 0036132209 scopus 로고    scopus 로고
    • SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases
    • Anantharaman V, Koonin EV, Aravind L. 2002. SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases. J Mol Microbiol Biotechnol 4: 71-75.
    • (2002) J Mol Microbiol Biotechnol , vol.4 , pp. 71-75
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 27
    • 0037526102 scopus 로고    scopus 로고
    • Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition
    • Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. 2003. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J 22: 2593-2603.
    • (2003) EMBO J , vol.22 , pp. 2593-2603
    • Ahn, H.J.1    Kim, H.W.2    Yoon, H.J.3    Lee, B.I.4    Suh, S.W.5    Yang, J.K.6
  • 30
    • 0001245587 scopus 로고
    • Nucleoside modification in archaebacterial transfer RNA
    • McCloskey J. 1986. Nucleoside modification in archaebacterial transfer RNA. Syst Appl Microbiol 7: 246-252.
    • (1986) Syst Appl Microbiol , vol.7 , pp. 246-252
    • McCloskey, J.1
  • 32
    • 0035853480 scopus 로고    scopus 로고
    • TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes
    • Anantharaman V, Koonin EV, Aravind L. 2001. TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes. FEMS Microbiol Lett 197: 215-221.
    • (2001) FEMS Microbiol Lett , vol.197 , pp. 215-221
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 34
    • 0024451607 scopus 로고
    • The selenocysteine-inserting opal suppressor serine tRNA from E coli is highly unusual in structure and modification.
    • Schön A, Böck A, Ott G, Sprinzl M, Söll D. 1989. The selenocysteine-inserting opal suppressor serine tRNA from E. coli is highly unusual in structure and modification. Nucleic Acids Res 17: 7159-7165.
    • (1989) Nucleic Acids Res , vol.17 , pp. 7159-7165
    • Schön, A.1    Böck, A.2    Ott, G.3    Sprinzl, M.4    Söll, D.5
  • 35
    • 0031571595 scopus 로고    scopus 로고
    • Three modified nucleosides present in the anticodon stem and loop influence the in vivo aa-tRNA selection in a tRNA-dependent manner
    • Li JN, Esberg B, Curran JF, Björk GR. 1997. Three modified nucleosides present in the anticodon stem and loop influence the in vivo aa-tRNA selection in a tRNA-dependent manner. J Mol Biol 271: 209-221.
    • (1997) J Mol Biol , vol.271 , pp. 209-221
    • Li, J.N.1    Esberg, B.2    Curran, J.F.3    Björk, G.R.4
  • 38
    • 0017840546 scopus 로고
    • The identification of the tRNA substrates for the supK tRNA methylase
    • Pope WT, Brown A, Reeves RH. 1978. The identification of the tRNA substrates for the supK tRNA methylase. Nucleic Acids Res 5: 1041-1057.
    • (1978) Nucleic Acids Res , vol.5 , pp. 1041-1057
    • Pope, W.T.1    Brown, A.2    Reeves, R.H.3
  • 39
    • 0022424144 scopus 로고
    • Nucleotide sequences of two serine tRNAs with a GGA anticodon:the structure-function relationships in the serine family of E coli tRNAs.
    • Grosjean H, Nicoghosian K, Haumont E, Söll D, Cedergren R. 1985. Nucleotide sequences of two serine tRNAs with a GGA anticodon:the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Res 13: 5697-5706.
    • (1985) Nucleic Acids Res , vol.13 , pp. 5697-5706
    • Grosjean, H.1    Nicoghosian, K.2    Haumont, E.3    Söll, D.4    Cedergren, R.5
  • 40
    • 0021112373 scopus 로고
    • Specific incorporation of selenium into lysineand glutamate-accepting tRNAs from Escherichia coli
    • Wittwer AJ. 1983. Specific incorporation of selenium into lysineand glutamate-accepting tRNAs from Escherichia coli. J Biol Chem 258: 8637-8641.
    • (1983) J Biol Chem , vol.258 , pp. 8637-8641
    • Wittwer, A.J.1
  • 41
    • 0024361792 scopus 로고
    • Lys from Escherichia coli: purification, codon specificity and translational activity
    • Lys from Escherichia coli: purification, codon specificity and translational activity. Biofactors 2: 27-34.
    • (1989) Biofactors , vol.2 , pp. 27-34
    • Wittwer, A.J.1    Ching, W.M.2
  • 42
    • 0021770891 scopus 로고
    • Identification and synthesis of a naturally occurring selenonucleoside in bacterial tRNAs: 5-:(methylamino)methyl:-2-selenouridine
    • Wittwer AJ, Tsai L, Ching WM, Stadtman TC. 1984. Identification and synthesis of a naturally occurring selenonucleoside in bacterial tRNAs: 5-:(methylamino)methyl:-2-selenouridine. Biochemistry 23: 4650-4655.
    • (1984) Biochemistry , vol.23 , pp. 4650-4655
    • Wittwer, A.J.1    Tsai, L.2    Ching, W.M.3    Stadtman, T.C.4
  • 44
    • 0018955991 scopus 로고
    • A novel link between the biosynthesis of aromatic amino acids and transfer RNA modification in Escherichia coli
    • Björk GR. 1980. A novel link between the biosynthesis of aromatic amino acids and transfer RNA modification in Escherichia coli. J Mol Biol 140: 391-410.
    • (1980) J Mol Biol , vol.140 , pp. 391-410
    • Björk, G.R.1
  • 45
    • 0036952614 scopus 로고    scopus 로고
    • Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli
    • Lauhon CT. 2002. Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli. J Bacteriol 184: 6820-6829.
    • (2002) J Bacteriol , vol.184 , pp. 6820-6829
    • Lauhon, C.T.1
  • 46
    • 0036955843 scopus 로고    scopus 로고
    • The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium
    • Nilsson K, Lundgren HK, Hagervall TG, Björk GR. 2002. The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium. J Bacteriol 184: 6830-6835.
    • (2002) J Bacteriol , vol.184 , pp. 6830-6835
    • Nilsson, K.1    Lundgren, H.K.2    Hagervall, T.G.3    Björk, G.R.4
  • 47
    • 1642541001 scopus 로고    scopus 로고
    • Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium occurs in two principally distinct pathways
    • Leipuviene R, Qian Q, Björk GR. 2004. Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium occurs in two principally distinct pathways. J Bacteriol 186: 758-766.
    • (2004) J Bacteriol , vol.186 , pp. 758-766
    • Leipuviene, R.1    Qian, Q.2    Björk, G.R.3
  • 48
    • 1342325436 scopus 로고    scopus 로고
    • Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine
    • Reader JS, Metzgar D, Schimmel P, De Crecy-Lagard V. 2004. Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine. J Biol Chem 279: 6280-6285.
    • (2004) J Biol Chem , vol.279 , pp. 6280-6285
    • Reader, J.S.1    Metzgar, D.2    Schimmel, P.3    De Crecy-Lagard, V.4
  • 49
    • 0031594815 scopus 로고    scopus 로고
    • 6-threonylcarbamoyladenosine in tRNA of Escherichia coli modestly improves the efficiency of the tRNA
    • 6-threonylcarbamoyladenosine in tRNA of Escherichia coli modestly improves the efficiency of the tRNA. J Bacteriol 180: 1808-1813.
    • (1998) J Bacteriol , vol.180 , pp. 1808-1813
    • Qian, Q.A.1    Curran, J.F.2    Björk, G.R.3
  • 50
    • 0019474499 scopus 로고
    • Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes
    • Ikemura T. 1981. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J Mol Biol 146: 1-21.
    • (1981) J Mol Biol , vol.146 , pp. 1-21
    • Ikemura, T.1
  • 51
    • 0025599976 scopus 로고
    • Growth rate dependence of transfer RNA abundance in Escherichia coli
    • Emilsson V, Kurland CG. 1990. Growth rate dependence of transfer RNA abundance in Escherichia coli. EMBO J 9: 4359-4366.
    • (1990) EMBO J , vol.9 , pp. 4359-4366
    • Emilsson, V.1    Kurland, C.G.2
  • 52
    • 0026727639 scopus 로고
    • Thiolation of transfer RNA in Escherichia coli varies with growth rate
    • Emilsson V, Näslund AK, Kurland CG. 1992. Thiolation of transfer RNA in Escherichia coli varies with growth rate. Nucleic Acids Res 20: 4499-4505.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4499-4505
    • Emilsson, V.1    Näslund, A.K.2    Kurland, C.G.3
  • 53
    • 0002495140 scopus 로고
    • Biosynthesis and function of modified nucleosides in tRNA
    • Söll D and UL RajBhandary (ed), ASM Press, Washington, D.C
    • Björk GR. 1995. Biosynthesis and function of modified nucleosides in tRNA, p 165-205. In Söll D and UL RajBhandary (ed), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 165-205
    • Björk, G.R.1
  • 54
    • 0001908381 scopus 로고    scopus 로고
    • Genetics and regulation of base modification in tRNA and rRNA of prokaryotes and eukaryotes
    • Grosjean H and Benne R (ed), ASM Press, Washington, D.C
    • Winkler ME. 1998. Genetics and regulation of base modification in tRNA and rRNA of prokaryotes and eukaryotes. In Grosjean H and Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA
    • Winkler, M.E.1
  • 55
    • 0015979238 scopus 로고
    • Biosynthesis of pseudouridine in transfer ribonucleic acid
    • Cortese R, Kammen HO, Spengler SJ, Ames BN. 1974. Biosynthesis of pseudouridine in transfer ribonucleic acid. J Biol Chem 249: 1103-1108.
    • (1974) J Biol Chem , vol.249 , pp. 1103-1108
    • Cortese, R.1    Kammen, H.O.2    Spengler, S.J.3    Ames, B.N.4
  • 56
    • 0023134503 scopus 로고
    • Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette
    • Arps PJ, Winkler ME. 1987. Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette. J Bacteriol 169: 1061-1070.
    • (1987) J Bacteriol , vol.169 , pp. 1061-1070
    • Arps, P.J.1    Winkler, M.E.2
  • 57
    • 0023645426 scopus 로고
    • The hisT-purF region of the Escherichia coli K-12 chromosome Identification of additional genes of the hisT and purF operons.
    • Nonet ML, Marvel CC, Tolan DR. 1987. The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J Biol Chem 262: 12209-12217.
    • (1987) J Biol Chem , vol.262 , pp. 12209-12217
    • Nonet, M.L.1    Marvel, C.C.2    Tolan, D.R.3
  • 58
    • 0024555369 scopus 로고
    • Transcription of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli
    • Bognar A, Pyne C, Yu M, Basi G. 1989. Transcription of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli. J Bacteriol 171: 1854-1861.
    • (1989) J Bacteriol , vol.171 , pp. 1854-1861
    • Bognar, A.1    Pyne, C.2    Yu, M.3    Basi, G.4
  • 59
    • 0024455262 scopus 로고
    • Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12
    • Schoenlein PV, Roa BB, Winkler ME. 1989. Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12. J Bacteriol 171: 6084-6092.
    • (1989) J Bacteriol , vol.171 , pp. 6084-6092
    • Schoenlein, P.V.1    Roa, B.B.2    Winkler, M.E.3
  • 60
    • 0023645566 scopus 로고
    • Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetasedihydrofolate synthetase product and regulation of expression by an upstream gene
    • Bognar AL, Osborne C, Shane B. 1987. Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetasedihydrofolate synthetase product and regulation of expression by an upstream gene. J Biol Chem 262: 12337-12343.
    • (1987) J Biol Chem , vol.262 , pp. 12337-12343
    • Bognar, A.L.1    Osborne, C.2    Shane, B.3
  • 61
    • 0024418098 scopus 로고
    • Differentially expressed trmD ribosomal protein operon of Escherichia coli is transcribed as a single polycistronic mRNA species
    • Byström AS, von Gabain A, Björk GR. 1989. Differentially expressed trmD ribosomal protein operon of Escherichia coli is transcribed as a single polycistronic mRNA species. J Mol Biol 208: 575-586.
    • (1989) J Mol Biol , vol.208 , pp. 575-586
    • Byström, A.S.1    von Gabain, A.2    Björk, G.R.3
  • 62
    • 0026020417 scopus 로고
    • The trmA promoter has regulatory features and sequence elements in common with the rRNA P1 promoter family of Escherichia coli
    • Gustafsson C, Lindström PH, Hagervall TG, Esberg KB, Björk GR. 1991. The trmA promoter has regulatory features and sequence elements in common with the rRNA P1 promoter family of Escherichia coli. J Bacteriol 173: 1757-1764.
    • (1991) J Bacteriol , vol.173 , pp. 1757-1764
    • Gustafsson, C.1    Lindström, P.H.2    Hagervall, T.G.3    Esberg, K.B.4    Björk, G.R.5
  • 63
    • 0018871116 scopus 로고
    • Promoter sequence for stringent control of bacterial ribonucleic acid synthesis
    • Travers A. 1980. Promoter sequence for stringent control of bacterial ribonucleic acid synthesis. J Bacteriol 141: 973-976.
    • (1980) J Bacteriol , vol.141 , pp. 973-976
    • Travers, A.1
  • 64
    • 0025838327 scopus 로고
    • Absence of hisT-mediated tRNA pseudouridylation results in a uracil requirement that interferes with Escherichia coli K-12 cell division
    • Tsui H-CT, Arps PJ, Connolly DM, Winkler ME. 1991. Absence of hisT-mediated tRNA pseudouridylation results in a uracil requirement that interferes with Escherichia coli K-12 cell division. J Bacteriol 173: 7395-7400.
    • (1991) J Bacteriol , vol.173 , pp. 7395-7400
    • Tsui, H.-C.T.1    Arps, P.J.2    Connolly, D.M.3    Winkler, M.E.4
  • 66
    • 0022356551 scopus 로고
    • Genetic organization and transcription from the gene (trmA) responsible for synthesis of tRNA (uracil-5)-methyltransferase by Escherichia coli
    • Lindström PH, Stüber D, Björk GR. 1985. Genetic organization and transcription from the gene (trmA) responsible for synthesis of tRNA (uracil-5)-methyltransferase by Escherichia coli. J Bacteriol 164: 1117-1123.
    • (1985) J Bacteriol , vol.164 , pp. 1117-1123
    • Lindström, P.H.1    Stüber, D.2    Björk, G.R.3
  • 67
    • 0025163439 scopus 로고
    • E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo.
    • Ross W, Thompson JF, Newlands JT, Gourse RL. 1990. E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J 9: 3733-3742.
    • (1990) EMBO J , vol.9 , pp. 3733-3742
    • Ross, W.1    Thompson, J.F.2    Newlands, J.T.3    Gourse, R.L.4
  • 68
    • 0025061514 scopus 로고
    • Potential binding sites of the trans-activator FIS are present upstream of all rRNA operons and of many but not all tRNA operons
    • Verbeek H, Nilsson L, Baliko G, Bosch L. 1990. Potential binding sites of the trans-activator FIS are present upstream of all rRNA operons and of many but not all tRNA operons. Biochim Biophys Acta 1050: 302-306.
    • (1990) Biochim Biophys Acta , vol.1050 , pp. 302-306
    • Verbeek, H.1    Nilsson, L.2    Baliko, G.3    Bosch, L.4
  • 69
    • 0024726281 scopus 로고
    • Identification of promoter mutants defective in growth-ratedependent regulation of rRNA transcription in Escherichia coli
    • Dickson RR, Gaal T, deBoer HA, deHaseth PL, Gourse RL. 1989. Identification of promoter mutants defective in growth-ratedependent regulation of rRNA transcription in Escherichia coli. J Bacteriol 171: 4862-4870.
    • (1989) J Bacteriol , vol.171 , pp. 4862-4870
    • Dickson, R.R.1    Gaal, T.2    deBoer, H.A.3    deHaseth, P.L.4    Gourse, R.L.5
  • 70
    • 0024383750 scopus 로고
    • Saturation mutagenesis of an Escherichia coli rRNA promoter and initial characterization of promoter variants
    • Gaal T, Barkei J, Dickson RR, deBoer HA, deHaseth PL, Alavi H, Gourse RL. 1989. Saturation mutagenesis of an Escherichia coli rRNA promoter and initial characterization of promoter variants. J Bacteriol 171: 4852-4861.
    • (1989) J Bacteriol , vol.171 , pp. 4852-4861
    • Gaal, T.1    Barkei, J.2    Dickson, R.R.3    deBoer, H.A.4    deHaseth, P.L.5    Alavi, H.6    Gourse, R.L.7
  • 71
    • 0018822181 scopus 로고
    • Growth rate-dependent regulation of transfer ribonucleic acid (5-methyluridine) methyltransferase in Escherichia coli B/r
    • Ny T, Björk GR. 1980. Growth rate-dependent regulation of transfer ribonucleic acid (5-methyluridine) methyltransferase in Escherichia coli B/r. J Bacteriol 141: 67-73.
    • (1980) J Bacteriol , vol.141 , pp. 67-73
    • Ny, T.1    Björk, G.R.2
  • 72
    • 0017373666 scopus 로고
    • 5U)methyltransferase from Escherichia coli
    • 5U)methyltransferase from Escherichia coli. J Bacteriol 130: 635-641.
    • (1977) J Bacteriol , vol.130 , pp. 635-641
    • Ny, T.1    Björk, G.R.2
  • 73
    • 0018974885 scopus 로고
    • Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic acid (5-methyluridine)- methyltransferase in Escherichia coli K-12
    • Ny T, Björk GR. 1980. Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic acid (5-methyluridine)- methyltransferase in Escherichia coli K-12. J Bacteriol 142: 371-379.
    • (1980) J Bacteriol , vol.142 , pp. 371-379
    • Ny, T.1    Björk, G.R.2
  • 74
    • 0027339112 scopus 로고
    • 5U54)-methyltransferase of Escherichia coli is present in two forms in vivo, one of which is present as bound to tRNA and to a 3′-end fragment of 16 S rRNA
    • 5U54)-methyltransferase of Escherichia coli is present in two forms in vivo, one of which is present as bound to tRNA and to a 3′-end fragment of 16 S rRNA. J Biol Chem 268: 1326-1331.
    • (1993) J Biol Chem , vol.268 , pp. 1326-1331
    • Gustafsson, C.1    Björk, G.R.2
  • 75
    • 0024084857 scopus 로고
    • Divergent promoters, a common form of gene organization
    • Beck CF, Warren RA. 1988. Divergent promoters, a common form of gene organization. Microbiol Rev 52: 318-326.
    • (1988) Microbiol Rev , vol.52 , pp. 318-326
    • Beck, C.F.1    Warren, R.A.2
  • 76
    • 0018141616 scopus 로고
    • Repression of synthesis of the vitamin B12 receptor in Escherichia coli
    • Kadner RJ. 1978. Repression of synthesis of the vitamin B12 receptor in Escherichia coli. J Bacteriol 136: 1050-1057.
    • (1978) J Bacteriol , vol.136 , pp. 1050-1057
    • Kadner, R.J.1
  • 79
    • 0023684123 scopus 로고
    • Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli
    • Wikström PM, Byström AS, Björk GR. 1988. Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli. J Mol Biol 203: 141-152.
    • (1988) J Mol Biol , vol.203 , pp. 141-152
    • Wikström, P.M.1    Byström, A.S.2    Björk, G.R.3
  • 80
    • 0024041831 scopus 로고
    • Noncoordinate translation-level regulation of ribosomal and nonribosomal protein genes in the Escherichia coli trmD operon
    • Wikström PM, Björk GR. 1988. Noncoordinate translation-level regulation of ribosomal and nonribosomal protein genes in the Escherichia coli trmD operon. J Bacteriol 170: 3025-3031.
    • (1988) J Bacteriol , vol.170 , pp. 3025-3031
    • Wikström, P.M.1    Björk, G.R.2
  • 81
    • 0026574167 scopus 로고
    • Importance of mRNA folding and start codon accessibility in the expression of genes in a ribosomal protein operon of Escherichia coli
    • Wikström PM, Lind LK, Berg DE, Björk GR. 1992. Importance of mRNA folding and start codon accessibility in the expression of genes in a ribosomal protein operon of Escherichia coli. J Mol Biol 224: 949-966.
    • (1992) J Mol Biol , vol.224 , pp. 949-966
    • Wikström, P.M.1    Lind, L.K.2    Berg, D.E.3    Björk, G.R.4
  • 82
    • 0018875554 scopus 로고
    • Noncoordinate regulation of enzymes involved in transfer RNA metabolism in Escherichia coli
    • Ny T, Thomale J, Hjalmarsson K, Nass G, Björk GR. 1980. Noncoordinate regulation of enzymes involved in transfer RNA metabolism in Escherichia coli. Biochim Biophys Acta 607: 277-284.
    • (1980) Biochim Biophys Acta , vol.607 , pp. 277-284
    • Ny, T.1    Thomale, J.2    Hjalmarsson, K.3    Nass, G.4    Björk, G.R.5
  • 83
    • 0027131291 scopus 로고
    • Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthiocis- ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants
    • Persson BC, Björk GR. 1993. Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthiocis- ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants. J Bacteriol 175: 7776-7785.
    • (1993) J Bacteriol , vol.175 , pp. 7776-7785
    • Persson, B.C.1    Björk, G.R.2
  • 84
    • 0028228191 scopus 로고
    • The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase
    • Tsui HCT, Zhao GS, Feng G, Leung HCE, Winkler ME. 1994. The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase. Mol Microbiol 11: 189-202.
    • (1994) Mol Microbiol , vol.11 , pp. 189-202
    • Tsui, H.C.T.1    Zhao, G.S.2    Feng, G.3    Leung, H.C.E.4    Winkler, M.E.5
  • 85
    • 0024076019 scopus 로고
    • Molecular cloning of the Escherichia coli miaA gene involved in the formation of delta 2-isopentenyl adenosine in tRNA
    • Caillet J, Droogmans L. 1988. Molecular cloning of the Escherichia coli miaA gene involved in the formation of delta 2-isopentenyl adenosine in tRNA. J Bacteriol 170: 4147-4152.
    • (1988) J Bacteriol , vol.170 , pp. 4147-4152
    • Caillet, J.1    Droogmans, L.2
  • 86
    • 0024371122 scopus 로고
    • 2-isopentenyl)- adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12
    • 2-isopentenyl)- adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J Bacteriol 171: 3233-3246.
    • (1989) J Bacteriol , vol.171 , pp. 3233-3246
    • Connolly, D.M.1    Winkler, M.E.2
  • 87
    • 0025974215 scopus 로고
    • Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations
    • Connolly DM, Winkler ME. 1991. Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations. J Bacteriol 173: 1711-1721.
    • (1991) J Bacteriol , vol.173 , pp. 1711-1721
    • Connolly, D.M.1    Winkler, M.E.2
  • 88
    • 0026067069 scopus 로고
    • Identification and sequence determination of the host factor gene for bacteriophage Q beta
    • Kajitani M, Ishihama A. 1991. Identification and sequence determination of the host factor gene for bacteriophage Q beta. Nucleic Acids Res 19: 1063-1066.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1063-1066
    • Kajitani, M.1    Ishihama, A.2
  • 91
    • 4344682527 scopus 로고    scopus 로고
    • The small RNA regulators of Escherichia coli:roles and mechanisms
    • Gottesman S. 2004. The small RNA regulators of Escherichia coli:roles and mechanisms. Annu Rev Microbiol 58: 303-328.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 303-328
    • Gottesman, S.1
  • 92
    • 0029889596 scopus 로고    scopus 로고
    • Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNAbinding protein encoded by the hfq gene
    • Brown L, Elliott T. 1996. Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNAbinding protein encoded by the hfq gene. J Bacteriol 178: 3763-3770.
    • (1996) J Bacteriol , vol.178 , pp. 3763-3770
    • Brown, L.1    Elliott, T.2
  • 93
    • 0030711638 scopus 로고    scopus 로고
    • Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12
    • Tsui HCT, Feng G, Winkler ME. 1997. Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12. J Bacteriol 179: 7476-7487.
    • (1997) J Bacteriol , vol.179 , pp. 7476-7487
    • Tsui, H.C.T.1    Feng, G.2    Winkler, M.E.3
  • 94
    • 0025893685 scopus 로고
    • Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes
    • Reuter K, Slany R, Ullrich F, Kersten H. 1991. Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes. J Bacteriol 173: 2256-2264.
    • (1991) J Bacteriol , vol.173 , pp. 2256-2264
    • Reuter, K.1    Slany, R.2    Ullrich, F.3    Kersten, H.4
  • 95
    • 0026739435 scopus 로고
    • The promoter of the tgt/sec operon in Escherichia coli is preceded by an upstream activation sequence that contains a high affinity FIS binding site
    • Slany RK, Kersten H. 1992. The promoter of the tgt/sec operon in Escherichia coli is preceded by an upstream activation sequence that contains a high affinity FIS binding site. Nucleic Acids Res 20: 4193-4198.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4193-4198
    • Slany, R.K.1    Kersten, H.2
  • 96
    • 1842404152 scopus 로고    scopus 로고
    • The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2′-O-methyltransferase activity
    • Persson BC, Jäger G, Gustafsson C. 1997. The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2′-O-methyltransferase activity. Nucleic Acids Res. 25: 4093-4097.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4093-4097
    • Persson, B.C.1    Jäger, G.2    Gustafsson, C.3
  • 97
    • 0027252959 scopus 로고
    • Guanylate kinase of Escherichia coli K-12
    • Gentry D, Bengra C, Ikehara K, Cashel M. 1993. Guanylate kinase of Escherichia coli K-12. J Biol Chem 268: 14316-14321.
    • (1993) J Biol Chem , vol.268 , pp. 14316-14321
    • Gentry, D.1    Bengra, C.2    Ikehara, K.3    Cashel, M.4
  • 98
    • 0026595482 scopus 로고
    • The nucleotide sequence of recG, the distal spo operon gene in Escherichia coli K-12
    • Kalman M, Murphy H, Cashel M. 1992. The nucleotide sequence of recG, the distal spo operon gene in Escherichia coli K-12. Gene 110: 95-99.
    • (1992) Gene , vol.110 , pp. 95-99
    • Kalman, M.1    Murphy, H.2    Cashel, M.3
  • 99
    • 0025790082 scopus 로고
    • Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12
    • Lloyd RG, Sharples GJ. 1991. Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12. J Bacteriol 173: 6837-6843.
    • (1991) J Bacteriol , vol.173 , pp. 6837-6843
    • Lloyd, R.G.1    Sharples, G.J.2
  • 101
    • 0024593347 scopus 로고
    • rpoZ, encoding the omega subunit of Escherichia coli RNA polymerase, is in the same operon as spoT
    • Gentry DR, Burgess RR. 1989. rpoZ, encoding the omega subunit of Escherichia coli RNA polymerase, is in the same operon as spoT. J Bacteriol 171: 1271-1277.
    • (1989) J Bacteriol , vol.171 , pp. 1271-1277
    • Gentry, D.R.1    Burgess, R.R.2
  • 102
    • 0016421339 scopus 로고
    • Biological methylation: selected aspects
    • Cantoni GL. 1975. Biological methylation: selected aspects. Annu Rev Biochem 44: 435-451.
    • (1975) Annu Rev Biochem , vol.44 , pp. 435-451
    • Cantoni, G.L.1
  • 103
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng XD, Roberts RJ. 2001. AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res 29: 3784-3795.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3784-3795
    • Cheng, X.D.1    Roberts, R.J.2
  • 104
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: a chronicle of convergence
    • Schubert HL, Blumenthal RM, Cheng X. 2003. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 28: 329-335.
    • (2003) Trends Biochem Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 105
    • 0020698678 scopus 로고
    • Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli
    • Hjalmarsson KJ, Byström AS, Björk GR. 1983. Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli. J Biol Chem 258: 1343-1351.
    • (1983) J Biol Chem , vol.258 , pp. 1343-1351
    • Hjalmarsson, K.J.1    Byström, A.S.2    Björk, G.R.3
  • 107
    • 0031581873 scopus 로고    scopus 로고
    • ProGGG of Salmonella typhimurium
    • ProGGG of Salmonella typhimurium. J Mol Biol 266: 283-296.
    • (1997) J Mol Biol , vol.266 , pp. 283-296
    • Qian, Q.1    Björk, G.R.2
  • 108
    • 0030678555 scopus 로고    scopus 로고
    • tRNA recognition for modification:solution probing of tRNA complexed with Escherichia coli tRNA (guanosine-1) methyltransferase
    • Gabryszuk J, Holmes WM. 1997. tRNA recognition for modification:solution probing of tRNA complexed with Escherichia coli tRNA (guanosine-1) methyltransferase. RNA 3: 1327-1336.
    • (1997) RNA , vol.3 , pp. 1327-1336
    • Gabryszuk, J.1    Holmes, W.M.2
  • 109
    • 0030811295 scopus 로고    scopus 로고
    • Interaction of tRNA with tRNA (guanosine-1)methyltransferase:binding specificity determinants involve the dinucleotide G(36)pG(37) and tertiary structure
    • Redlak M, AndraosSelim C, Giege R, Florentz C, Holmes WM. 1997. Interaction of tRNA with tRNA (guanosine-1)methyltransferase:binding specificity determinants involve the dinucleotide G(36)pG(37) and tertiary structure. Biochemistry 36: 8699-8709.
    • (1997) Biochemistry , vol.36 , pp. 8699-8709
    • Redlak, M.1    AndraosSelim, C.2    Giege, R.3    Florentz, C.4    Holmes, W.M.5
  • 110
    • 0141592367 scopus 로고    scopus 로고
    • Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 A resolution: a novel methyltransferase fold
    • Liu J, Wang W, Shin DH, Yokota H, Kim R, Kim SH. 2003. Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 A resolution: a novel methyltransferase fold. Proteins 53: 326-328.
    • (2003) Proteins , vol.53 , pp. 326-328
    • Liu, J.1    Wang, W.2    Shin, D.H.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 111
    • 0019226833 scopus 로고
    • 5U-methyltransferase from Escherichia coli
    • 5U-methyltransferase from Escherichia coli. J Biol Chem 255: 8296-8302.
    • (1980) J Biol Chem , vol.255 , pp. 8296-8302
    • Greenberg, R.1    Dudock, B.2
  • 115
    • 0023667711 scopus 로고
    • Catalytic mechanism and inhibition of tRNA (uracil-5-)methyltransferase: evidence for covalent catalysis
    • Santi DV, Hardy LW. 1987. Catalytic mechanism and inhibition of tRNA (uracil-5-)methyltransferase: evidence for covalent catalysis. Biochemistry 26: 8599-8606.
    • (1987) Biochemistry , vol.26 , pp. 8599-8606
    • Santi, D.V.1    Hardy, L.W.2
  • 117
    • 0028650333 scopus 로고
    • Enzymatic mechanism of tRNA (m(5)u54)methyltransferase
    • Kealey JT, Gu X, Santi DV. 1994. Enzymatic mechanism of tRNA (m(5)u54)methyltransferase. Biochimie 76: 1133-1142.
    • (1994) Biochimie , vol.76 , pp. 1133-1142
    • Kealey, J.T.1    Gu, X.2    Santi, D.V.3
  • 118
    • 0031113361 scopus 로고    scopus 로고
    • The dynamic NMR structure of the T psi C-loop: implications for the specificity of tRNA methylation
    • Yao LJ, James TL, Kealey JT, Santi DV, Schmitz U. 1997. The dynamic NMR structure of the T psi C-loop: implications for the specificity of tRNA methylation. J Biomol NMR 9: 229-244.
    • (1997) J Biomol NMR , vol.9 , pp. 229-244
    • Yao, L.J.1    James, T.L.2    Kealey, J.T.3    Santi, D.V.4    Schmitz, U.5
  • 119
    • 0345096517 scopus 로고    scopus 로고
    • The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate
    • Foster PG, Nunes CR, Greene P, Moustakas D, Stroud RM. 2003. The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate. Structure (Cambridge) 11: 1609-1620.
    • (2003) Structure (Cambridge) , vol.11 , pp. 1609-1620
    • Foster, P.G.1    Nunes, C.R.2    Greene, P.3    Moustakas, D.4    Stroud, R.M.5
  • 120
    • 0037125961 scopus 로고    scopus 로고
    • RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine
    • King MY, Redman KL. 2002. RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine. Biochemistry 41: 11218-11225.
    • (2002) Biochemistry , vol.41 , pp. 11218-11225
    • King, M.Y.1    Redman, K.L.2
  • 121
    • 0034682446 scopus 로고    scopus 로고
    • m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts
    • Liu Y, Santi DV. 2000. m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts. Proc Natl Acad Sci USA 97: 8263-8265.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8263-8265
    • Liu, Y.1    Santi, D.V.2
  • 122
    • 3343024377 scopus 로고    scopus 로고
    • Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA
    • Bujnicki JM, Oudjama Y, Roovers M, Owczarek S, Caillet J, Droogmans L. 2004. Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. RNA 10: 1236-1242.
    • (2004) RNA , vol.10 , pp. 1236-1242
    • Bujnicki, J.M.1    Oudjama, Y.2    Roovers, M.3    Owczarek, S.4    Caillet, J.5    Droogmans, L.6
  • 123
    • 1342307414 scopus 로고    scopus 로고
    • The conserved Cys-X(1)-X(2)-Cys motif present in the TtcA protein is required for the thiolation of cytidine in position 32 of tRNA from Salmonella enterica serovar Typhimurium
    • Jäger G, Leipuviene R, Pollard MG, Qian Q, Björk GR. 2004. The conserved Cys-X(1)-X(2)-Cys motif present in the TtcA protein is required for the thiolation of cytidine in position 32 of tRNA from Salmonella enterica serovar Typhimurium. J Bacteriol 186: 750-757.
    • (2004) J Bacteriol , vol.186 , pp. 750-757
    • Jäger, G.1    Leipuviene, R.2    Pollard, M.G.3    Qian, Q.4    Björk, G.R.5
  • 125
    • 0029786633 scopus 로고    scopus 로고
    • Recognition of the Tarm of tRNA by tRNA (m(5)U54)-methyltransferase is not sequence specific
    • Gu XR, Ivanetich KM, Santi DV. 1996. Recognition of the Tarm of tRNA by tRNA (m(5)U54)-methyltransferase is not sequence specific. Biochemistry 35: 11652-11659.
    • (1996) Biochemistry , vol.35 , pp. 11652-11659
    • Gu, X.R.1    Ivanetich, K.M.2    Santi, D.V.3
  • 126
    • 0034653278 scopus 로고    scopus 로고
    • Modified constructs of the tRNA T Psi C domain to probe substrate conformational requirements of m(1)A(58) and m(5)U(54) tRNA methyltransferases
    • Sengupta R, Vainauskas S, Yarian C, Sochacka E, Malkiewicz A, Guenther RH, Koshlap KM, Agris PF. 2000. Modified constructs of the tRNA T Psi C domain to probe substrate conformational requirements of m(1)A(58) and m(5)U(54) tRNA methyltransferases. Nucleic Acids Res 28: 1374-1380.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1374-1380
    • Sengupta, R.1    Vainauskas, S.2    Yarian, C.3    Sochacka, E.4    Malkiewicz, A.5    Guenther, R.H.6    Koshlap, K.M.7    Agris, P.F.8
  • 127
    • 0014667184 scopus 로고
    • 6N (gamma,gamma, dimethylallyl) adenosine in transfer RNA of Escherichia coli
    • 6N (gamma,gamma, dimethylallyl) adenosine in transfer RNA of Escherichia coli. Biochem Biophys Res Commun 36: 435-441.
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 435-441
    • Gefter, M.L.1
  • 128
    • 0020479290 scopus 로고
    • A thermostable tRNA (guanosine-2′)-methyltransferase from Thermus thermophilus HB27 and the effect of ribose methylation on the conformational stability of tRNA
    • Kumagai I, Watanabe K, Oshima T. 1982. A thermostable tRNA (guanosine-2′)-methyltransferase from Thermus thermophilus HB27 and the effect of ribose methylation on the conformational stability of tRNA. J Biol Chem 257: 7388-7395.
    • (1982) J Biol Chem , vol.257 , pp. 7388-7395
    • Kumagai, I.1    Watanabe, K.2    Oshima, T.3
  • 129
    • 1842607227 scopus 로고    scopus 로고
    • Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
    • Nureki O, Watanabe K, Fukai S, Ishii R, Endo Y, Hori H, Yokoyama S. 2004. Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme. Structure (Cambridge) 12: 593-602.
    • (2004) Structure (Cambridge) , vol.12 , pp. 593-602
    • Nureki, O.1    Watanabe, K.2    Fukai, S.3    Ishii, R.4    Endo, Y.5    Hori, H.6    Yokoyama, S.7
  • 130
    • 0036206498 scopus 로고    scopus 로고
    • Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs
    • Hori H, Suzuki T, Sugawara K, Inoue Y, Shibata T, Kuramitsu S, Yokoyama S, Oshima T, Watanabe K. 2002. Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs. Genes Cells 7: 259-272.
    • (2002) Genes Cells , vol.7 , pp. 259-272
    • Hori, H.1    Suzuki, T.2    Sugawara, K.3    Inoue, Y.4    Shibata, T.5    Kuramitsu, S.6    Yokoyama, S.7    Oshima, T.8    Watanabe, K.9
  • 132
    • 0024824294 scopus 로고
    • Effects of modification of 4-thiouridine in E coli tRNA(fMet) on its methyl acceptor activity by thermostable Gm-methylases.
    • Hori H, Saneyoshi M, Kumagai I, Miura K, Watanabe K. 1989. Effects of modification of 4-thiouridine in E. coli tRNA(fMet) on its methyl acceptor activity by thermostable Gm-methylases. J Biochem (Tokyo) 106: 798-802.
    • (1989) J Biochem (Tokyo) , vol.106 , pp. 798-802
    • Hori, H.1    Saneyoshi, M.2    Kumagai, I.3    Miura, K.4    Watanabe, K.5
  • 134
    • 0023970985 scopus 로고
    • Thionucleosides in transfer ribonucleic acid: diversity, structure, biosynthesis, and function
    • Ajitkumar P, Cherayil JD. 1988. Thionucleosides in transfer ribonucleic acid: diversity, structure, biosynthesis, and function. Microbiol Rev 52: 103-113.
    • (1988) Microbiol Rev , vol.52 , pp. 103-113
    • Ajitkumar, P.1    Cherayil, J.D.2
  • 135
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz CJ, Giel JL, Patschkowski T, Luther C, Ruzicka FJ, Beinert H, Kiley PJ. 2001. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc Natl Acad Sci USA 98: 14895-14900.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 137
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • Urbina HD, Silberg JJ, Hoff KG, Vickery LE. 2001. Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. J Biol Chem 276: 44521-44526.
    • (2001) J Biol Chem , vol.276 , pp. 44521-44526
    • Urbina, H.D.1    Silberg, J.J.2    Hoff, K.G.3    Vickery, L.E.4
  • 138
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • Ollagnier-de-Choudens S, Mattioli T, Takahashi Y, Fontecave M. 2001. Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. J Biol Chem 276: 22604-22607.
    • (2001) J Biol Chem , vol.276 , pp. 22604-22607
    • Ollagnier-de-Choudens, S.1    Mattioli, T.2    Takahashi, Y.3    Fontecave, M.4
  • 139
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the ironsulfur cluster template protein IscU
    • Hoff KG, Ta DT, Tapley TL, Silberg JJ, Vickery LE. 2002. Hsc66 substrate specificity is directed toward a discrete region of the ironsulfur cluster template protein IscU. J Biol Chem 277: 27353-27359.
    • (2002) J Biol Chem , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 140
    • 2442538132 scopus 로고    scopus 로고
    • Substitutions in an active site loop of escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo
    • Lauhon CT, Skovran E, Urbina HD, Downs DM, Vickery LE. 2004. Substitutions in an active site loop of escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo. J Biol Chem 279: 19551-19558.
    • (2004) J Biol Chem , vol.279 , pp. 19551-19558
    • Lauhon, C.T.1    Skovran, E.2    Urbina, H.D.3    Downs, D.M.4    Vickery, L.E.5
  • 141
    • 0015239003 scopus 로고
    • The biosynthesis of 4-thiouridylate Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system
    • Abrell JW, Kaufman EE, Lipsett MN. 1971. The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system. J Biol Chem 246: 294-301.
    • (1971) J Biol Chem , vol.246 , pp. 294-301
    • Abrell, J.W.1    Kaufman, E.E.2    Lipsett, M.N.3
  • 142
    • 0018129631 scopus 로고
    • Enzymes producing 4-thiouridine in Escherichia coli tRNA: approximate chromosomal locations of the genes and enzyme activities in a 4-thiouridine-deficient mutant
    • Lipsett MN. 1978. Enzymes producing 4-thiouridine in Escherichia coli tRNA: approximate chromosomal locations of the genes and enzyme activities in a 4-thiouridine-deficient mutant. J Bacteriol 135: 993-997.
    • (1978) J Bacteriol , vol.135 , pp. 993-997
    • Lipsett, M.N.1
  • 143
    • 0019944780 scopus 로고
    • Isolation of single-site Escherichia coli mutants deficient in thiamine and 4-thiouridine syntheses: identification of a nuvC mutant
    • Ryals J, Hsu RY, Lipsett MN, Bremer H. 1982. Isolation of single-site Escherichia coli mutants deficient in thiamine and 4-thiouridine syntheses: identification of a nuvC mutant. J Bacteriol 151: 899-904.
    • (1982) J Bacteriol , vol.151 , pp. 899-904
    • Ryals, J.1    Hsu, R.Y.2    Lipsett, M.N.3    Bremer, H.4
  • 145
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint DH. 1996. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J Biol Chem 271: 16068-16074.
    • (1996) J Biol Chem , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 146
    • 0034646676 scopus 로고    scopus 로고
    • Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati R, Lauhon CT. 2000. Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. J Biol Chem 275: 10727-10730.
    • (2000) J Biol Chem , vol.275 , pp. 10727-10730
    • Kambampati, R.1    Lauhon, C.T.2
  • 147
    • 0034708503 scopus 로고    scopus 로고
    • Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate
    • Palenchar PM, Buck CJ, Cheng H, Larson TJ, Mueller EG. 2000. Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J Biol Chem 275: 8283-8286.
    • (2000) J Biol Chem , vol.275 , pp. 8283-8286
    • Palenchar, P.M.1    Buck, C.J.2    Cheng, H.3    Larson, T.J.4    Mueller, E.G.5
  • 148
    • 0028559230 scopus 로고
    • A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity
    • Bork P, Koonin EV. 1994. A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. Proteins 20: 347-355.
    • (1994) Proteins , vol.20 , pp. 347-355
    • Bork, P.1    Koonin, E.V.2
  • 149
    • 0035823572 scopus 로고    scopus 로고
    • The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA
    • Mueller EG, Palenchar PM, Buck CJ. 2001. The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA. J Biol Chem 276: 33588-33595.
    • (2001) J Biol Chem , vol.276 , pp. 33588-33595
    • Mueller, E.G.1    Palenchar, P.M.2    Buck, C.J.3
  • 150
    • 0036432968 scopus 로고    scopus 로고
    • A paradigm for biological sulfur transfers via persulfide groups: a persulfide-disulfidethiol cycle in 4-thiouridine biosynthesis
    • Wright CM, Palenchar PM, Mueller EG. 2002. A paradigm for biological sulfur transfers via persulfide groups: a persulfide-disulfidethiol cycle in 4-thiouridine biosynthesis. Chem Commun 22: 2708-2709.
    • (2002) Chem Commun , vol.22 , pp. 2708-2709
    • Wright, C.M.1    Palenchar, P.M.2    Mueller, E.G.3
  • 151
    • 2542426480 scopus 로고    scopus 로고
    • Substrate specificity for 4-thiouridine modification in Escherichia coli
    • Lauhon CT, Erwin WM, Ton GN. 2004. Substrate specificity for 4-thiouridine modification in Escherichia coli. J Biol Chem 279: 23022-23029.
    • (2004) J Biol Chem , vol.279 , pp. 23022-23029
    • Lauhon, C.T.1    Erwin, W.M.2    Ton, G.N.3
  • 152
    • 0021770444 scopus 로고
    • Novel coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine.
    • Elseviers D, Petrullo LA, Gallagher PJ. 1984. Novel . coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine. Nucleic Acids Res 12: 3521-3534.
    • (1984) Nucleic Acids Res , vol.12 , pp. 3521-3534
    • Elseviers, D.1    Petrullo, L.A.2    Gallagher, P.J.3
  • 153
    • 0023664535 scopus 로고
    • Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities
    • Hagervall TG, Edmonds CG, McCloskey JA, Björk GR. 1987. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. J Biol Chem 262: 8488-8495.
    • (1987) J Biol Chem , vol.262 , pp. 8488-8495
    • Hagervall, T.G.1    Edmonds, C.G.2    McCloskey, J.A.3    Björk, G.R.4
  • 154
    • 0037417771 scopus 로고    scopus 로고
    • MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli
    • Kambampati R, Lauhon CT. 2003. MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli. Biochemistry 42: 1109-1117.
    • (2003) Biochemistry , vol.42 , pp. 1109-1117
    • Kambampati, R.1    Lauhon, C.T.2
  • 155
    • 0021941805 scopus 로고
    • Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine
    • Sullivan MA, Cannon JF, Webb FH, Bock RM. 1985. Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine. J Bacteriol 161: 368-376.
    • (1985) J Bacteriol , vol.161 , pp. 368-376
    • Sullivan, M.A.1    Cannon, J.F.2    Webb, F.H.3    Bock, R.M.4
  • 156
    • 0043210520 scopus 로고    scopus 로고
    • The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function
    • Yim L, Martínez-Vicente M, Villarroya M, Aguado C, Knecht E, Armengod ME. 2003. The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. J Biol Chem 278: 28378-28387.
    • (2003) J Biol Chem , vol.278 , pp. 28378-28387
    • Yim, L.1    Martínez-Vicente, M.2    Villarroya, M.3    Aguado, C.4    Knecht, E.5    Armengod, M.E.6
  • 157
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift
    • Bregeon D, Colot V, Radman M, Taddei F. 2001. Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev 15: 2295-2306.
    • (2001) Genes Dev , vol.15 , pp. 2295-2306
    • Bregeon, D.1    Colot, V.2    Radman, M.3    Taddei, F.4
  • 158
    • 0034762265 scopus 로고    scopus 로고
    • GidA is an FAD-binding protein involved in development of Myxococcus xanthus
    • White DJ, Merod R, Thomasson B, Hartzell PL. 2001. GidA is an FAD-binding protein involved in development of Myxococcus xanthus. Mol Microbiol 42: 503-517.
    • (2001) Mol Microbiol , vol.42 , pp. 503-517
    • White, D.J.1    Merod, R.2    Thomasson, B.3    Hartzell, P.L.4
  • 159
    • 0033573089 scopus 로고    scopus 로고
    • The Escherichia coli trmE (MnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties
    • Cabedo H, Macian F, Villarroya M, Escudero JC, MartinezVicente M, Knecht E, Armengod ME. 1999. The Escherichia coli trmE (MnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties. EMBO J 18: 7063-7076.
    • (1999) EMBO J , vol.18 , pp. 7063-7076
    • Cabedo, H.1    Macian, F.2    Villarroya, M.3    Escudero, J.C.4    MartinezVicente, M.5    Knecht, E.6    Armengod, M.E.7
  • 160
    • 13244284641 scopus 로고    scopus 로고
    • The structure of the TrmE GTP-binding protein and its implications for tRNA modification
    • Scrima A, Vetter IR, Armengod ME, Wittinghofer A. 2005. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J 24: 23-33.
    • (2005) EMBO J , vol.24 , pp. 23-33
    • Scrima, A.1    Vetter, I.R.2    Armengod, M.E.3    Wittinghofer, A.4
  • 161
    • 0032561194 scopus 로고    scopus 로고
    • MTO1 codes for a mitochondrial protein required for respiration in paromomycin-resistant mutants of Saccharomyces cerevisiae
    • Colby G, Wu M, Tzagoloff A. 1998. MTO1 codes for a mitochondrial protein required for respiration in paromomycin-resistant mutants of Saccharomyces cerevisiae. J Biol Chem 273: 27945-27952.
    • (1998) J Biol Chem , vol.273 , pp. 27945-27952
    • Colby, G.1    Wu, M.2    Tzagoloff, A.3
  • 163
    • 0345826117 scopus 로고    scopus 로고
    • Functional diversity of the Rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphatedependent tRNA 2-selenouridine synthase
    • Wolfe MD, Ahmed F, Lacourciere GM, Lauhon CT, Stadtman TC, Larson TJ. 2004. Functional diversity of the Rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphatedependent tRNA 2-selenouridine synthase. J Biol Chem 279: 1801-1809.
    • (2004) J Biol Chem , vol.279 , pp. 1801-1809
    • Wolfe, M.D.1    Ahmed, F.2    Lacourciere, G.M.3    Lauhon, C.T.4    Stadtman, T.C.5    Larson, T.J.6
  • 165
    • 0023954987 scopus 로고
    • Isolation and characterization of a selenium metabolism mutant of Salmonella typhimurium
    • Kramer GF, Ames BN. 1988. Isolation and characterization of a selenium metabolism mutant of Salmonella typhimurium. J Bacteriol 170: 736-743.
    • (1988) J Bacteriol , vol.170 , pp. 736-743
    • Kramer, G.F.1    Ames, B.N.2
  • 166
    • 0022502192 scopus 로고
    • Biosynthesis of 5- methylaminomethyl-2-selenouridine, a naturally occurring nucleoside in Escherichia coli tRNA
    • Wittwer AJ, Stadtman TC. 1986. Biosynthesis of 5- methylaminomethyl-2-selenouridine, a naturally occurring nucleoside in Escherichia coli tRNA. Arch Biochem Biophys 248: 540-550.
    • (1986) Arch Biochem Biophys , vol.248 , pp. 540-550
    • Wittwer, A.J.1    Stadtman, T.C.2
  • 167
    • 0027144016 scopus 로고
    • Monoselenophosphate - synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound sepx
    • Glass RS, Singh WP, Jung W, Veres Z, Scholz TD, Stadtman TC. 1993. Monoselenophosphate - synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound sepx. Biochemistry 32: 12555-12559.
    • (1993) Biochemistry , vol.32 , pp. 12555-12559
    • Glass, R.S.1    Singh, W.P.2    Jung, W.3    Veres, Z.4    Scholz, T.D.5    Stadtman, T.C.6
  • 168
    • 0028289519 scopus 로고
    • Selenophosphate synthetase-enzyme properties and catalytic reaction
    • Veres Z, Kim IY, Scholz TD, Stadtman TC. 1994. Selenophosphate synthetase-enzyme properties and catalytic reaction. J Biol Chem 269: 10597-10603.
    • (1994) J Biol Chem , vol.269 , pp. 10597-10603
    • Veres, Z.1    Kim, I.Y.2    Scholz, T.D.3    Stadtman, T.C.4
  • 169
    • 0028144791 scopus 로고
    • A purified selenophosphatedependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium
    • Veres Z, Stadtman TC. 1994. A purified selenophosphatedependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium. Proc Natl Acad Sci USA 91: 8092-8096.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8092-8096
    • Veres, Z.1    Stadtman, T.C.2
  • 170
    • 0018572506 scopus 로고
    • The effect of an Escherichia coli regulatory mutation on transfer RNA structure
    • Eisenberg SP, Yarus M, Soll L. 1979. The effect of an Escherichia coli regulatory mutation on transfer RNA structure. J Mol Biol 135: 111-126.
    • (1979) J Mol Biol , vol.135 , pp. 111-126
    • Eisenberg, S.P.1    Yarus, M.2    Soll, L.3
  • 171
    • 0022655673 scopus 로고
    • Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2
    • Ericson JU, Björk GR. 1986. Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2. J Bacteriol 166: 1013-1021.
    • (1986) J Bacteriol , vol.166 , pp. 1013-1021
    • Ericson, J.U.1    Björk, G.R.2
  • 172
    • 0030926773 scopus 로고    scopus 로고
    • Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12
    • Leung HCE, Chen YQ, Winkler ME. 1997. Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12. J Biol Chem 272: 13073-13083.
    • (1997) J Biol Chem , vol.272 , pp. 13073-13083
    • Leung, H.C.E.1    Chen, Y.Q.2    Winkler, M.E.3
  • 173
    • 0031019672 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme
    • Moore JA, Poulter CD. 1997. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme. Biochemistry 36: 604-614.
    • (1997) Biochemistry , vol.36 , pp. 604-614
    • Moore, J.A.1    Poulter, C.D.2
  • 174
    • 0034732888 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop
    • Soderberg T, Poulter CD. 2000. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. Biochemistry 39: 6546-6553.
    • (2000) Biochemistry , vol.39 , pp. 6546-6553
    • Soderberg, T.1    Poulter, C.D.2
  • 175
    • 0035852848 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: site-directed mutagenesis of highly conserved residues
    • Soderberg T, Poulter CD. 2001. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: site-directed mutagenesis of highly conserved residues. Biochemistry 40: 1734-1740.
    • (2001) Biochemistry , vol.40 , pp. 1734-1740
    • Soderberg, T.1    Poulter, C.D.2
  • 176
    • 0021049671 scopus 로고
    • Sequence specificity of tRNA-modifying enzymes An analysis of 258 tRNA sequences
    • Tsang TH, Buck M, Ames BN. 1983. Sequence specificity of tRNA-modifying enzymes. An analysis of 258 tRNA sequences. Biochim Biophys Acta 741: 180-196.
    • (1983) Biochim Biophys Acta , vol.741 , pp. 180-196
    • Tsang, T.H.1    Buck, M.2    Ames, B.N.3
  • 177
    • 0030750024 scopus 로고    scopus 로고
    • Transfer RNA recognition by the Escherichia coli Delta(2)-isopentenylpyrophosphate:tRNA Delta 2-isopentenyl transferase: dependence on the anticodon arm structure
    • Motorin Y, Bec G, Tewari R, Grosjean H. 1997. Transfer RNA recognition by the Escherichia coli Delta(2)-isopentenylpyrophosphate:tRNA Delta 2-isopentenyl transferase: dependence on the anticodon arm structure. RNA 3: 721-733.
    • (1997) RNA , vol.3 , pp. 721-733
    • Motorin, Y.1    Bec, G.2    Tewari, R.3    Grosjean, H.4
  • 178
    • 0028986353 scopus 로고
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA. J Bacteriol 177: 1967-1975.
    • (1995) J Bacteriol , vol.177 , pp. 1967-1975
    • Esberg, B.1    Björk, G.R.2
  • 180
    • 0017819272 scopus 로고
    • 2-isopentenyl)-adenosine during growth of enteropathogenic Escherichia coli in the presence of ironbinding proteins
    • 2-isopentenyl)-adenosine during growth of enteropathogenic Escherichia coli in the presence of ironbinding proteins. Eur J Biochem 82: 503-513.
    • (1978) Eur J Biochem , vol.82 , pp. 503-513
    • Griffiths, E.1    Humphreys, J.2
  • 181
    • 0014694355 scopus 로고
    • An iron-dependent modification of several transfer RNA species in Escherichia coli
    • Rosenberg AH, Gefter ML. 1969. An iron-dependent modification of several transfer RNA species in Escherichia coli. J Mol Biol 46: 581-584.
    • (1969) J Mol Biol , vol.46 , pp. 581-584
    • Rosenberg, A.H.1    Gefter, M.L.2
  • 182
    • 0014433423 scopus 로고
    • Physiologically induced changes in the property of phenylalanine tRNA in Escherichia coli
    • Wettstein FO, Stent GS. 1968. Physiologically induced changes in the property of phenylalanine tRNA in Escherichia coli. J Mol Biol 38: 25-40.
    • (1968) J Mol Biol , vol.38 , pp. 25-40
    • Wettstein, F.O.1    Stent, G.S.2
  • 183
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms:functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, ReyesSpindola JF, Miller NE. 2001. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms:functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29: 1097-1106.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    ReyesSpindola, J.F.4    Miller, N.E.5
  • 184
    • 0037134469 scopus 로고    scopus 로고
    • Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
    • Pierrel F, Björk GR, Fontecave M, Atta M. 2002. Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J Biol Chem 277: 13367-13370.
    • (2002) J Biol Chem , vol.277 , pp. 13367-13370
    • Pierrel, F.1    Björk, G.R.2    Fontecave, M.3    Atta, M.4
  • 185
    • 0043032766 scopus 로고    scopus 로고
    • MiaB protein from Thermotoga maritima Characterization of an extremely thermophilic tRNA-methylthiotransferase
    • Pierrel F, Hernandez HL, Johnson MK, Fontecave M, Atta M. 2003. MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. J Biol Chem 278: 29515-29524.
    • (2003) J Biol Chem , vol.278 , pp. 29515-29524
    • Pierrel, F.1    Hernandez, H.L.2    Johnson, M.K.3    Fontecave, M.4    Atta, M.5
  • 187
    • 9144220291 scopus 로고    scopus 로고
    • MiaB protein is a bifunctional "Radical SAM" enzyme involved in thiolation and methylation of tRNA
    • Pierrel F, Douki T, Fontecave M, Atta M. 2004. MiaB protein is a bifunctional "Radical SAM" enzyme involved in thiolation and methylation of tRNA. J Biol Chem 279: 47555-47563.
    • (2004) J Biol Chem , vol.279 , pp. 47555-47563
    • Pierrel, F.1    Douki, T.2    Fontecave, M.3    Atta, M.4
  • 188
    • 0020491144 scopus 로고
    • 6A) is present in the transfer RNA of Salmonella typhimurium, but not Escherichia coli
    • 6A) is present in the transfer RNA of Salmonella typhimurium, but not Escherichia coli. Nucleic Acids Res 10: 5649-5662.
    • (1982) Nucleic Acids Res , vol.10 , pp. 5649-5662
    • Buck, M.1    McCloskey, J.A.2    Basile, B.3    Ames, B.N.4
  • 189
    • 0021256993 scopus 로고
    • A modified nucleotide in tRNA as a possible regulator of aerobiosis: synthesis of cis-2-methylthioribosylzeatin in the tRNA of Salmonella
    • Buck M, Ames BN. 1984. A modified nucleotide in tRNA as a possible regulator of aerobiosis: synthesis of cis-2-methylthioribosylzeatin in the tRNA of Salmonella. Cell 36: 523-531.
    • (1984) Cell , vol.36 , pp. 523-531
    • Buck, M.1    Ames, B.N.2
  • 192
    • 9644273984 scopus 로고    scopus 로고
    • P-site pairing subtleties revealed by the effects of different tRNAs on programmed translational bypassing where anticodon re-pairing to mRNA is separated from dissociation
    • Bucklin DJ, Wills NM, Gesteland RF, Atkins JF. 2005. P-site pairing subtleties revealed by the effects of different tRNAs on programmed translational bypassing where anticodon re-pairing to mRNA is separated from dissociation. J Mol Biol 345: 39-49.
    • (2005) J Mol Biol , vol.345 , pp. 39-49
    • Bucklin, D.J.1    Wills, N.M.2    Gesteland, R.F.3    Atkins, J.F.4
  • 193
    • 0025348395 scopus 로고
    • Suppression of the negative effect of minor arginine codons on gene expression; preferential usage of minor codons within the first 25 codons of the Escherichia coli genes
    • Chen GF, Inouye M. 1990. Suppression of the negative effect of minor arginine codons on gene expression; preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res 18: 1465-1473.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1465-1473
    • Chen, G.F.1    Inouye, M.2
  • 194
    • 0029313081 scopus 로고
    • A dual-specificity pseudouridine synthase-an Escherichia coli synthase purified and cloned on the basis of its specificity for psi-746 in 23S RNA is also specific for psi-32 in tRNA(Phe)
    • Wrzesinski J, Nurse K, Bakin A, Lane BG, Ofengand J. 1995. A dual-specificity pseudouridine synthase-an Escherichia coli synthase purified and cloned on the basis of its specificity for psi-746 in 23S RNA is also specific for psi-32 in tRNA(Phe). RNA 1: 437-448.
    • (1995) RNA , vol.1 , pp. 437-448
    • Wrzesinski, J.1    Nurse, K.2    Bakin, A.3    Lane, B.G.4    Ofengand, J.5
  • 195
    • 0029832294 scopus 로고    scopus 로고
    • Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes
    • Gustafsson C, Reid R, Greene PJ, Santi DV. 1996. Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes. Nucleic Acids Res 24: 3756-3762.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3756-3762
    • Gustafsson, C.1    Reid, R.2    Greene, P.J.3    Santi, D.V.4
  • 196
    • 0029945504 scopus 로고    scopus 로고
    • Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases
    • Koonin EV. 1996. Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Res 24: 2411-2415.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 197
    • 0038475918 scopus 로고    scopus 로고
    • A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya
    • Kaya Y, Ofengand J. 2003. A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya. RNA 9: 711-721.
    • (2003) RNA , vol.9 , pp. 711-721
    • Kaya, Y.1    Ofengand, J.2
  • 198
    • 1642580818 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli
    • Del Campo M, Ofengand J, Malhotra A. 2004. Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli. RNA 10: 231-239.
    • (2004) RNA , vol.10 , pp. 231-239
    • Del Campo, M.1    Ofengand, J.2    Malhotra, A.3
  • 199
    • 0033987499 scopus 로고    scopus 로고
    • The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I
    • Foster PG, Huang L, Santi DV, Stroud RM. 2000. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat Struct Biol 7: 23-27.
    • (2000) Nat Struct Biol , vol.7 , pp. 23-27
    • Foster, P.G.1    Huang, L.2    Santi, D.V.3    Stroud, R.M.4
  • 200
    • 2442450595 scopus 로고    scopus 로고
    • Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold
    • Kaya Y, Del Campo M, Ofengand J, Malhotra A. 2004. Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold. J Biol Chem 279: 18107-18110.
    • (2004) J Biol Chem , vol.279 , pp. 18107-18110
    • Kaya, Y.1    Del Campo, M.2    Ofengand, J.3    Malhotra, A.4
  • 201
    • 0017393706 scopus 로고
    • Biosynthesis of pseudouridine in the in vitro transcribed tRNATyr precursor
    • Ciampi MS, Arena F, Cortese R. 1977. Biosynthesis of pseudouridine in the in vitro transcribed tRNATyr precursor. FEBS Lett 77: 75-82.
    • (1977) FEBS Lett , vol.77 , pp. 75-82
    • Ciampi, M.S.1    Arena, F.2    Cortese, R.3
  • 202
    • 0014857203 scopus 로고
    • In vitro biosynthesis of pseudouridine at the polynucleotide level by an enzyme extract from Escherichia coli
    • Johnson L, Söll D. 1970. In vitro biosynthesis of pseudouridine at the polynucleotide level by an enzyme extract from Escherichia coli. Proc Natl Acad Sci USA 67: 943-950.
    • (1970) Proc Natl Acad Sci USA , vol.67 , pp. 943-950
    • Johnson, L.1    Söll, D.2
  • 203
    • 0033435203 scopus 로고    scopus 로고
    • The mechanism of pseudouridine synthase I as deduced from its interaction with 5- fluorouracil-tRNA
    • Gu XR, Liu YQ, Santi DV. 1999. The mechanism of pseudouridine synthase I as deduced from its interaction with 5- fluorouracil-tRNA. Proc Natl Acad Sci USA 96: 14270-14275.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14270-14275
    • Gu, X.R.1    Liu, Y.Q.2    Santi, D.V.3
  • 204
    • 0032488657 scopus 로고    scopus 로고
    • A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst
    • Huang LX, Pookanjanatavip M, Gu XG, Santi DV. 1998. A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst. Biochemistry 37: 344-351.
    • (1998) Biochemistry , vol.37 , pp. 344-351
    • Huang, L.X.1    Pookanjanatavip, M.2    Gu, X.G.3    Santi, D.V.4
  • 205
    • 0023851755 scopus 로고
    • Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I
    • Kammen HO, Marvel CC, Hardy L, Penhoet EE. 1988. Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I. J Biol Chem 263: 2255-2263.
    • (1988) J Biol Chem , vol.263 , pp. 2255-2263
    • Kammen, H.O.1    Marvel, C.C.2    Hardy, L.3    Penhoet, E.E.4
  • 206
    • 0242331664 scopus 로고    scopus 로고
    • Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
    • Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM. 2003. Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc Natl Acad Sci USA 100: 12648-12653.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12648-12653
    • Pan, H.1    Agarwalla, S.2    Moustakas, D.T.3    Finer-Moore, J.4    Stroud, R.M.5
  • 207
    • 0031565927 scopus 로고    scopus 로고
    • Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the T Psi-loop of yeast tRNAs
    • Becker HF, Motorin Y, Sissler M, Florentz C, Grosjean H. 1997. Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the T Psi-loop of yeast tRNAs. J Mol Biol 274: 505-518.
    • (1997) J Mol Biol , vol.274 , pp. 505-518
    • Becker, H.F.1    Motorin, Y.2    Sissler, M.3    Florentz, C.4    Grosjean, H.5
  • 208
    • 0032488604 scopus 로고    scopus 로고
    • Molecular recognition of tRNA by tRNA pseudouridine 55 synthase
    • Gu XR, Yu M, Ivanetich KM, Santi DV. 1998. Molecular recognition of tRNA by tRNA pseudouridine 55 synthase. Biochemistry 37: 339-343.
    • (1998) Biochemistry , vol.37 , pp. 339-343
    • Gu, X.R.1    Yu, M.2    Ivanetich, K.M.3    Santi, D.V.4
  • 209
    • 0034547125 scopus 로고    scopus 로고
    • Deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells
    • Gutgsell N, Englund N, Niu LH, Kaya Y, Lane BG, Ofengand J. 2000. Deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells. RNA 6: 1870-1881.
    • (2000) RNA , vol.6 , pp. 1870-1881
    • Gutgsell, N.1    Englund, N.2    Niu, L.H.3    Kaya, Y.4    Lane, B.G.5    Ofengand, J.6
  • 210
    • 0018074482 scopus 로고
    • Purification of pseudouridylate synthetase I from Salmonella typhimurium
    • Arena F, Ciliberto G, Ciampi S, Cortese R. 1978. Purification of pseudouridylate synthetase I from Salmonella typhimurium. Nucleic Acids Res 5: 4523-4536.
    • (1978) Nucleic Acids Res , vol.5 , pp. 4523-4536
    • Arena, F.1    Ciliberto, G.2    Ciampi, S.3    Cortese, R.4
  • 211
    • 0031914957 scopus 로고    scopus 로고
    • Characterization of yeast protein Deg1 as pseudouridine synthase (Pus3) catalyzing the formation of Psi(38) and Psi(39) in tRNA anticodon loop
    • Lecointe F, Simos G, Sauer A, Hurt EC, Motorin Y, Grosjean H. 1998. Characterization of yeast protein Deg1 as pseudouridine synthase (Pus3) catalyzing the formation of Psi(38) and Psi(39) in tRNA anticodon loop. J Biol Chem 273: 1316-1323.
    • (1998) J Biol Chem , vol.273 , pp. 1316-1323
    • Lecointe, F.1    Simos, G.2    Sauer, A.3    Hurt, E.C.4    Motorin, Y.5    Grosjean, H.6
  • 212
    • 0035163770 scopus 로고    scopus 로고
    • Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli
    • Del Campo M, Kaya Y, Ofengand J. 2001. Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli. RNA 7: 1603-1615.
    • (2001) RNA , vol.7 , pp. 1603-1615
    • Del Campo, M.1    Kaya, Y.2    Ofengand, J.3
  • 214
    • 4644266760 scopus 로고    scopus 로고
    • Procmo5UGG promotes reading of all four proline codons in vivo
    • Procmo5UGG promotes reading of all four proline codons in vivo. RNA 10: 1662-1673.
    • (2004) RNA , vol.10 , pp. 1662-1673
    • Näsvall, S.J.1    Chen, P.2    Björk, G.R.3
  • 215
    • 0018189383 scopus 로고
    • Purification and characterization of a tRNA methylase from Salmonella typhimurium
    • Pope WT, Reeves RH. 1978. Purification and characterization of a tRNA methylase from Salmonella typhimurium. J Bacteriol 136: 191-200.
    • (1978) J Bacteriol , vol.136 , pp. 191-200
    • Pope, W.T.1    Reeves, R.H.2
  • 216
    • 0016831438 scopus 로고
    • Transfer ribonucleic acid methylase deficiency found in UGA supressor strains
    • Reeves RH, Roth JR. 1975. Transfer ribonucleic acid methylase deficiency found in UGA supressor strains. J Bacteriol 124: 332-340.
    • (1975) J Bacteriol , vol.124 , pp. 332-340
    • Reeves, R.H.1    Roth, J.R.2
  • 217
    • 0024060925 scopus 로고
    • Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli
    • Kawakami K, Jönsson YH, Björk GR, Ikeda H, Nakamura Y. 1988. Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli. Proc Natl Acad Sci USA 85: 5620-5624.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5620-5624
    • Kawakami, K.1    Jönsson, Y.H.2    Björk, G.R.3    Ikeda, H.4    Nakamura, Y.5
  • 218
  • 219
    • 0018800830 scopus 로고
    • Novel mechanism of post-transcriptional modification of tRNA Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction
    • Okada N, Noguchi S, Kasai H, Shindo-Okada N, Ohgi T, Goto T, Nishimura S. 1979. Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction. J Biol Chem 254: 3067-3073.
    • (1979) J Biol Chem , vol.254 , pp. 3067-3073
    • Okada, N.1    Noguchi, S.2    Kasai, H.3    Shindo-Okada, N.4    Ohgi, T.5    Goto, T.6    Nishimura, S.7
  • 220
    • 0036952706 scopus 로고    scopus 로고
    • An unexpected absence of queuosine modification in the tRNAs of an Escherichia coli B strain
    • Dineshkumar TK, Thanedar S, Subbulakshmi C, Varshney U. 2002. An unexpected absence of queuosine modification in the tRNAs of an Escherichia coli B strain. Microbiology 148: 3779-3787.
    • (2002) Microbiology , vol.148 , pp. 3779-3787
    • Dineshkumar, T.K.1    Thanedar, S.2    Subbulakshmi, C.3    Varshney, U.4
  • 221
    • 0018125687 scopus 로고
    • Isolation of Q nucleoside precursor present in tRNA of an coli mutant and its characterization as 7- (cyano)-7-deazaguanosine.
    • Noguchi S, Yamaizumi Z, Ohgi T, Goto T, Nishimura Y, Hirota Y, Nishimura S. 1978. Isolation of Q nucleoside precursor present in tRNA of an . coli mutant and its characterization as 7- (cyano)-7-deazaguanosine. Nucleic Acids Res 5: 4215-4223.
    • (1978) Nucleic Acids Res , vol.5 , pp. 4215-4223
    • Noguchi, S.1    Yamaizumi, Z.2    Ohgi, T.3    Goto, T.4    Nishimura, Y.5    Hirota, Y.6    Nishimura, S.7
  • 223
    • 0017570364 scopus 로고
    • Detection of nucleoside Q precursor in methyl-deficient E.coli tRNA
    • Okada N, Yasuda T, Nishimura S. 1977. Detection of nucleoside Q precursor in methyl-deficient E.coli tRNA. Nucleic Acids Res 4: 4063-4075.
    • (1977) Nucleic Acids Res , vol.4 , pp. 4063-4075
    • Okada, N.1    Yasuda, T.2    Nishimura, S.3
  • 224
    • 4644221389 scopus 로고    scopus 로고
    • Aminoacylation of the anticodon stem by a tRNA-synthetase paralog: relic of an ancient code? Trends Biochem
    • Grosjean H, de Crécy-Lagard V, Björk GR. 2004. Aminoacylation of the anticodon stem by a tRNA-synthetase paralog: relic of an ancient code? Trends Biochem. Sci. 29: 519-522.
    • (2004) Sci. , vol.29 , pp. 519-522
    • Grosjean, H.1    de Crécy-Lagard, V.2    Björk, G.R.3
  • 225
    • 0029991713 scopus 로고    scopus 로고
    • Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
    • Romier C, Reuter K, Suck D, Ficner R. 1996. Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange. EMBO J 15: 2850-2857.
    • (1996) EMBO J , vol.15 , pp. 2850-2857
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 226
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
    • Xie W, Liu X, Huang RH. 2003. Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat Struct Biol 10: 781-788.
    • (2003) Nat Struct Biol , vol.10 , pp. 781-788
    • Xie, W.1    Liu, X.2    Huang, R.H.3
  • 227
    • 0035960560 scopus 로고    scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli: molecular mechanism and role of aspartate 89
    • Kittendorf JD, Barcomb LM, Nonekowski ST, Garcia GA. 2001. tRNA-guanine transglycosylase from Escherichia coli: molecular mechanism and role of aspartate 89. Biochemistry 40: 14123-14133.
    • (2001) Biochemistry , vol.40 , pp. 14123-14133
    • Kittendorf, J.D.1    Barcomb, L.M.2    Nonekowski, S.T.3    Garcia, G.A.4
  • 228
    • 0029754654 scopus 로고    scopus 로고
    • Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase reveal aspartate 102 as the active site nucleophile
    • Romier C, Reuter K, Suck D, Ficner R. 1996. Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase reveal aspartate 102 as the active site nucleophile. Biochemistry 35: 15734-15739.
    • (1996) Biochemistry , vol.35 , pp. 15734-15739
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 229
    • 0029116609 scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli - minimal tRNA structure and sequence requirements for recognition
    • Curnow AW, Garcia GA. 1995. tRNA-guanine transglycosylase from Escherichia coli - minimal tRNA structure and sequence requirements for recognition. J Biol Chem 270: 17264-17267.
    • (1995) J Biol Chem , vol.270 , pp. 17264-17267
    • Curnow, A.W.1    Garcia, G.A.2
  • 230
    • 0028595685 scopus 로고
    • A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNAguanine transglycosylase
    • Nakanishi S, Ueda T, Hori H, Yamazaki N, Okada N, Watanabe K. 1994. A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNAguanine transglycosylase. J Biol Chem 269: 32221-32225.
    • (1994) J Biol Chem , vol.269 , pp. 32221-32225
    • Nakanishi, S.1    Ueda, T.2    Hori, H.3    Yamazaki, N.4    Okada, N.5    Watanabe, K.6
  • 231
    • 0037310429 scopus 로고    scopus 로고
    • Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA
    • Iwata-Reuyl D. 2003. Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA. Bioorg Chem 31: 24-43.
    • (2003) Bioorg Chem , vol.31 , pp. 24-43
    • Iwata-Reuyl, D.1
  • 232
    • 0027295625 scopus 로고
    • A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine
    • Slany RK, Bösl M, Crain PF, Kersten H. 1993. A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. Biochemistry 32: 7811-7817.
    • (1993) Biochemistry , vol.32 , pp. 7811-7817
    • Slany, R.K.1    Bösl, M.2    Crain, P.F.3    Kersten, H.4
  • 233
    • 0038193526 scopus 로고    scopus 로고
    • tRNA modification by S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA): assay development and characterization of the recombinant enzyme
    • Van Lanen SG, Daoud Kinzie S, Matthieu S, Link T, Culp J, Iwata-Reuyl D. 2003. tRNA modification by S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA): assay development and characterization of the recombinant enzyme. J Biol Chem 278: 10491-10499.
    • (2003) J Biol Chem , vol.278 , pp. 10491-10499
    • Van Lanen, S.G.1    Daoud Kinzie, S.2    Matthieu, S.3    Link, T.4    Culp, J.5    Iwata-Reuyl, D.6
  • 234
    • 0023903154 scopus 로고
    • New function of vitamin B12: cobamide-dependent reduction of epoxyqueuosine to queuosine in tRNAs of Escherichia coli and Salmonella typhimurium
    • Frey B, McCloskey J, Kersten W, Kersten H. 1988. New function of vitamin B12: cobamide-dependent reduction of epoxyqueuosine to queuosine in tRNAs of Escherichia coli and Salmonella typhimurium. J Bacteriol 170: 2078-2082.
    • (1988) J Bacteriol , vol.170 , pp. 2078-2082
    • Frey, B.1    McCloskey, J.2    Kersten, W.3    Kersten, H.4
  • 235
    • 11144357971 scopus 로고    scopus 로고
    • Aminoacyl-tRNAs: setting the limits of the genetic code
    • Ibba M, Söll D. 2004. Aminoacyl-tRNAs: setting the limits of the genetic code. Genes Dev 18: 731-738.
    • (2004) Genes Dev , vol.18 , pp. 731-738
    • Ibba, M.1    Söll, D.2
  • 236
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • Schimmel P, Ribas De Pouplana L. 2000. Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem Sci 25: 207-209.
    • (2000) Trends Biochem Sci , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 239
    • 0036792830 scopus 로고    scopus 로고
    • tRNomics: analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodon- sparing strategies and domain-specific features
    • Marck C, Grosjean H. 2002. tRNomics: analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodon- sparing strategies and domain-specific features. RNA 8: 1189-1232.
    • (2002) RNA , vol.8 , pp. 1189-1232
    • Marck, C.1    Grosjean, H.2
  • 242
    • 0001580215 scopus 로고
    • Nucleotide sequences in the yeast alanine transfer ribonucleic acid
    • Holley RW, Everett GA, Madison JT, Zamir A. 1965. Nucleotide sequences in the yeast alanine transfer ribonucleic acid. J Biol Chem 240: 2122-2128.
    • (1965) J Biol Chem , vol.240 , pp. 2122-2128
    • Holley, R.W.1    Everett, G.A.2    Madison, J.T.3    Zamir, A.4
  • 243
    • 0013936167 scopus 로고
    • Codon-anticodon pairing The wobble hypothesis
    • Crick FHC. 1966. Codon-anticodon pairing. The wobble hypothesis. J Mol Biol 19: 548-555.
    • (1966) J Mol Biol , vol.19 , pp. 548-555
    • Crick, F.H.C.1
  • 244
    • 0011895723 scopus 로고    scopus 로고
    • Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA
    • Auxilien S, Crain PF, Trewyn RW, Grosjean H. 1996. Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA. J Mol Biol 262: 437-458.
    • (1996) J Mol Biol , vol.262 , pp. 437-458
    • Auxilien, S.1    Crain, P.F.2    Trewyn, R.W.3    Grosjean, H.4
  • 245
    • 0033527628 scopus 로고    scopus 로고
    • An adenosine deaminase that generates inosine at the wobble position of tRNAs
    • Gerber AP, Keller W. 1999. An adenosine deaminase that generates inosine at the wobble position of tRNAs. Science 286: 1146-1149.
    • (1999) Science , vol.286 , pp. 1146-1149
    • Gerber, A.P.1    Keller, W.2
  • 246
    • 0037099742 scopus 로고    scopus 로고
    • tadA, an essential tRNAspecific adenosine deaminase from Escherichia coli
    • Wolf J, Gerber AP, Keller W. 2002. tadA, an essential tRNAspecific adenosine deaminase from Escherichia coli. EMBO J 21: 3841-3851.
    • (2002) EMBO J , vol.21 , pp. 3841-3851
    • Wolf, J.1    Gerber, A.P.2    Keller, W.3
  • 247
    • 0036295962 scopus 로고    scopus 로고
    • A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine
    • Chen P, Qian Q, Zhang S, Isaksson LA, Björk GR. 2002. A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine. J Mol Biol 317: 481-492.
    • (2002) J Mol Biol , vol.317 , pp. 481-492
    • Chen, P.1    Qian, Q.2    Zhang, S.3    Isaksson, L.A.4    Björk, G.R.5
  • 248
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giege R, Sissler M, Florentz C. 1998. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res 26: 5017-5035.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5017-5035
    • Giege, R.1    Sissler, M.2    Florentz, C.3
  • 249
    • 85054214571 scopus 로고
    • The role of modified nucleosides in tRNA interactions
    • Hatfield DL, Lee BJ, and Pirtle RM (ed), CRC Press, Boca Raton, Fla
    • Björk GR. 1992. The role of modified nucleosides in tRNA interactions, p 23-85. In Hatfield DL, Lee BJ, and Pirtle RM (ed), Transfer RNA in Protein Synthesis. CRC Press, Boca Raton, Fla.
    • (1992) Transfer RNA in Protein Synthesis , pp. 23-85
    • Björk, G.R.1
  • 250
  • 253
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson JR, Uhlenbeck OC. 1988. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc Natl Acad Sci USA 85: 1033-1037.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 254
    • 0026587432 scopus 로고
    • Recognition of tertiary structure in tRNAs by Rh(phen)2phi3+, a new reagent for RNA structure-function mapping
    • Chow CS, Behlen LS, Uhlenbeck OC, Barton JK. 1992. Recognition of tertiary structure in tRNAs by Rh(phen)2phi3+, a new reagent for RNA structure-function mapping. Biochemistry 31: 972-982.
    • (1992) Biochemistry , vol.31 , pp. 972-982
    • Chow, C.S.1    Behlen, L.S.2    Uhlenbeck, O.C.3    Barton, J.K.4
  • 256
    • 0025267036 scopus 로고
    • Relaxation of a transfer RNA specificity by removal of modified nucleotides
    • Perret V, Garcia A, Grosjean H, Ebel JP, Florentz C, Giege R. 1990. Relaxation of a transfer RNA specificity by removal of modified nucleotides. Nature 344: 787-789.
    • (1990) Nature , vol.344 , pp. 787-789
    • Perret, V.1    Garcia, A.2    Grosjean, H.3    Ebel, J.P.4    Florentz, C.5    Giege, R.6
  • 257
    • 0024277927 scopus 로고
    • Anticodon switching changes the identity of methionine and valine transfer RNAs
    • Schulman LH, Pelka H. 1988. Anticodon switching changes the identity of methionine and valine transfer RNAs. Science 242: 765-768.
    • (1988) Science , vol.242 , pp. 765-768
    • Schulman, L.H.1    Pelka, H.2
  • 258
    • 0030816674 scopus 로고    scopus 로고
    • The modified wobble base inosine in yeast tRNA(Ile) is a positive determinant for aminoacylation by isoleucyl tRNA synthetase
    • Senger B, Auxilien S, Englisch U, Cramer F, Fasiolo F. 1997. The modified wobble base inosine in yeast tRNA(Ile) is a positive determinant for aminoacylation by isoleucyl tRNA synthetase. Biochemistry 36: 8269-8275.
    • (1997) Biochemistry , vol.36 , pp. 8269-8275
    • Senger, B.1    Auxilien, S.2    Englisch, U.3    Cramer, F.4    Fasiolo, F.5
  • 259
    • 0023734317 scopus 로고
    • Codon and aminoacid specificities of a transfer RNA are both converted by a single posttranscriptional modification
    • Muramatsu T, Nishikawa K, Nemoto F, Kuchino Y, Nishimura S, Miyazawa T, Yokoyama S. 1988. Codon and aminoacid specificities of a transfer RNA are both converted by a single posttranscriptional modification. Nature 336: 179-181.
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3    Kuchino, Y.4    Nishimura, S.5    Miyazawa, T.6    Yokoyama, S.7
  • 260
    • 0021100683 scopus 로고
    • Base substitutions in the wobble position of the anticodon inhibit aminoacylation of E coli tRNAfMet by E coli Met-tRNA synthetase.
    • Schulman LH, Pelka H, Susani M. 1983. Base substitutions in the wobble position of the anticodon inhibit aminoacylation of E. coli tRNAfMet by E coli Met-tRNA synthetase. Nucleic Acids Res 11: 1439-1455.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1439-1455
    • Schulman, L.H.1    Pelka, H.2    Susani, M.3
  • 261
    • 0017752733 scopus 로고
    • Role of anticodon bases in aminoacylation of Escherichia coli methionine transfer RNAs
    • Stern L, Schulman LH. 1977. Role of anticodon bases in aminoacylation of Escherichia coli methionine transfer RNAs. J Biol Chem 252: 6403-6408.
    • (1977) J Biol Chem , vol.252 , pp. 6403-6408
    • Stern, L.1    Schulman, L.H.2
  • 262
    • 0026581038 scopus 로고
    • Recognition of the nucleoside in the first position of the anticodon of isoleucine tRNA by isoleucyl-tRNA synthetase from Escherichia coli
    • Muramatsu T, Miyazawa T, Yokoyama S. 1992. Recognition of the nucleoside in the first position of the anticodon of isoleucine tRNA by isoleucyl-tRNA synthetase from Escherichia coli. Nucl Nucl 11: 719-730.
    • (1992) Nucl Nucl , vol.11 , pp. 719-730
    • Muramatsu, T.1    Miyazawa, T.2    Yokoyama, S.3
  • 263
    • 0015221041 scopus 로고
    • Selective inactivation of amino acid acceptor and ribosome-binding activities of Escherichia coli tRNA by modification with cyanogen bromide
    • Saneyoshi M, Nishimura S. 1971. Selective inactivation of amino acid acceptor and ribosome-binding activities of Escherichia coli tRNA by modification with cyanogen bromide. Biochim Biophys Acta 246: 123-131.
    • (1971) Biochim Biophys Acta , vol.246 , pp. 123-131
    • Saneyoshi, M.1    Nishimura, S.2
  • 265
    • 0029907152 scopus 로고    scopus 로고
    • The crystal structures of T-thermophilus lysyl-tRNA synthetase complexed with E-coli tRNA(Lys) and a T-thermophilus tRNA(Lys) transcript: anticodon recognition and conformational changes upon binding of a lysyladenylate analogue
    • Cusack S, Yaremchuk A, Tukalo M. 1996. The crystal structures of T-thermophilus lysyl-tRNA synthetase complexed with E-coli tRNA(Lys) and a T-thermophilus tRNA(Lys) transcript: anticodon recognition and conformational changes upon binding of a lysyladenylate analogue. EMBO J 15: 6321-6334.
    • (1996) EMBO J , vol.15 , pp. 6321-6334
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 266
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould MA, Perona JJ, Steitz TA. 1991. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352: 213-218.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 267
    • 0015868989 scopus 로고
    • Biological function of 2- thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid
    • Agris PF, Söll D, Seno T. 1973. Biological function of 2- thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry 12: 4331-4337.
    • (1973) Biochemistry , vol.12 , pp. 4331-4337
    • Agris, P.F.1    Söll, D.2    Seno, T.3
  • 269
    • 0033572751 scopus 로고    scopus 로고
    • Effect of modified nucleotides on Escherichia coli tRNA(Glu) structure and on its aminoacylation by glutamyl-tRNA synthetase-predominant and distinct roles of the mnm(5) and s(2) modifications of U34
    • Madore E, Florentz C, Giege R, Sekine S, Yokoyama S, Lapointe J. 1999. Effect of modified nucleotides on Escherichia coli tRNA(Glu) structure and on its aminoacylation by glutamyl-tRNA synthetase-predominant and distinct roles of the mnm(5) and s(2) modifications of U34. Eur J Biochem 266: 1128-1135.
    • (1999) Eur J Biochem , vol.266 , pp. 1128-1135
    • Madore, E.1    Florentz, C.2    Giege, R.3    Sekine, S.4    Yokoyama, S.5    Lapointe, J.6
  • 270
    • 0041490850 scopus 로고    scopus 로고
    • Aminoacylation of hypomodified tRNA(Glu) in vivo
    • Kruger MK, Sorensen MA. 1998. Aminoacylation of hypomodified tRNA(Glu) in vivo. J Mol Biol 284: 609-620.
    • (1998) J Mol Biol , vol.284 , pp. 609-620
    • Kruger, M.K.1    Sorensen, M.A.2
  • 271
    • 0015242224 scopus 로고
    • 6-isopentenyladenosine and lack of disulfide formation.
    • 6-isopentenyladenosine and lack of disulfide formation. Biochim Biophys Acta 238: 464-474.
    • (1971) Biochim Biophys Acta , vol.238 , pp. 464-474
    • Faulkner, R.D.1    Uziel, M.2
  • 272
    • 0019872063 scopus 로고
    • The effect upon aminoacylation of bisulphite addition to 2-methylthio-N6-isopentenyl adenosine of Escherichia coli phenylalanine tRNA
    • Goddard JP, Lowdon M. 1981. The effect upon aminoacylation of bisulphite addition to 2-methylthio-N6-isopentenyl adenosine of Escherichia coli phenylalanine tRNA. FEBS Lett 130: 221-222.
    • (1981) FEBS Lett , vol.130 , pp. 221-222
    • Goddard, J.P.1    Lowdon, M.2
  • 273
    • 0014674092 scopus 로고
    • Role of modifications in tyrosine transfer RNA: a modified base affecting ribosome binding
    • Gefter ML, Russell RL. 1969. Role of modifications in tyrosine transfer RNA: a modified base affecting ribosome binding. J Mol Biol 39: 145-157.
    • (1969) J Mol Biol , vol.39 , pp. 145-157
    • Gefter, M.L.1    Russell, R.L.2
  • 274
    • 0000036468 scopus 로고
    • 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA
    • 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA. Proc Natl Acad Sci USA 86: 409-413.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 409-413
    • Wilson, R.K.1    Roe, B.A.2
  • 278
    • 0000960472 scopus 로고
    • On the physical basis for ambiguity in genetic coding interactions
    • Grosjean HJ, de Henau S, Crothers DM. 1978. On the physical basis for ambiguity in genetic coding interactions. Proc Natl Acad Sci USA 75: 610-614.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 610-614
    • Grosjean, H.J.1    de Henau, S.2    Crothers, D.M.3
  • 279
    • 0019913580 scopus 로고
    • Translational efficiency of transfer RNAs: uses of an extended anticodon
    • Yarus M. 1982. Translational efficiency of transfer RNAs: uses of an extended anticodon. Science 218: 646-652.
    • (1982) Science , vol.218 , pp. 646-652
    • Yarus, M.1
  • 280
    • 0033600832 scopus 로고    scopus 로고
    • Singly and bifurcated hydrogenbonded base-pairs in tRNA anticodon hairpins and ribozymes
    • Auffinger P, Westhof E. 1999. Singly and bifurcated hydrogenbonded base-pairs in tRNA anticodon hairpins and ribozymes. J Mol Biol 292: 467-483.
    • (1999) J Mol Biol , vol.292 , pp. 467-483
    • Auffinger, P.1    Westhof, E.2
  • 281
    • 0022382412 scopus 로고
    • Analysis of modification-dependent structural alterations in the anticodon loop of Escherichia coli tRNAArg and their effects on the translation of MS2 RNA
    • Baumann U, Fischer W, Sprinzl M. 1985. Analysis of modification-dependent structural alterations in the anticodon loop of Escherichia coli tRNAArg and their effects on the translation of MS2 RNA. Eur J Biochem 152: 645-649.
    • (1985) Eur J Biochem , vol.152 , pp. 645-649
    • Baumann, U.1    Fischer, W.2    Sprinzl, M.3
  • 283
    • 0002157687 scopus 로고
    • Modified nucleosides in tRNA
    • Schimmel PR, Söll D, and Abelson JN (ed), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y
    • Nishimura S. 1979. Modified nucleosides in tRNA, p 59-79. In Schimmel PR, Söll D, and Abelson JN (ed), Transfer RNA: Structure, Properties, and Recognition. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1979) Transfer RNA: Structure, Properties, and Recognition , pp. 59-79
    • Nishimura, S.1
  • 284
    • 0000635454 scopus 로고
    • Thiolation of uridine carbon-2 restricts the motional dynamics of the transfer RNA wobble position nucleoside
    • Agris PF, Sierzputowska-Gracz H, Smith W, Malkiewicz A, Sochacka E, Nawrot B. 1992. Thiolation of uridine carbon-2 restricts the motional dynamics of the transfer RNA wobble position nucleoside. J Am Chem Soc 114: 2652-2656.
    • (1992) J Am Chem Soc , vol.114 , pp. 2652-2656
    • Agris, P.F.1    Sierzputowska-Gracz, H.2    Smith, W.3    Malkiewicz, A.4    Sochacka, E.5    Nawrot, B.6
  • 287
    • 0029894141 scopus 로고    scopus 로고
    • NMR studies of the effects of the 5′-phosphate group on conformational properties of 5-methylaminomethyluridine found in the first position of the anticodon of Escherichia coli tRNA(Arg)4
    • Sakamoto K, Kawai G, Watanabe S, Niimi T, Hayashi N, Muto Y, Watanabe K, Satoh T, Sekine M, Yokoyama S. 1996. NMR studies of the effects of the 5′-phosphate group on conformational properties of 5-methylaminomethyluridine found in the first position of the anticodon of Escherichia coli tRNA(Arg)4. Biochemistry 35: 6533-6538.
    • (1996) Biochemistry , vol.35 , pp. 6533-6538
    • Sakamoto, K.1    Kawai, G.2    Watanabe, S.3    Niimi, T.4    Hayashi, N.5    Muto, Y.6    Watanabe, K.7    Satoh, T.8    Sekine, M.9    Yokoyama, S.10
  • 288
    • 0034680364 scopus 로고    scopus 로고
    • Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical Uturn structure
    • Sundaram M, Durant PC, Davis DR. 2000. Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical Uturn structure. Biochemistry 39: 12575-12584.
    • (2000) Biochemistry , vol.39 , pp. 12575-12584
    • Sundaram, M.1    Durant, P.C.2    Davis, D.R.3
  • 289
    • 0345531141 scopus 로고    scopus 로고
    • Roles of 5-substituents of tRNA wobble uridines in the recognition of purine-ending codons
    • Takai K, Yokoyama S. 2003. Roles of 5-substituents of tRNA wobble uridines in the recognition of purine-ending codons. Nucleic Acids Res 31: 6383-6391.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6383-6391
    • Takai, K.1    Yokoyama, S.2
  • 290
    • 0026343194 scopus 로고
    • Wobble position modified nucleosides evolved to select transfer RNA codon recognition: a modified-wobble hypothesis
    • Agris PF. 1991. Wobble position modified nucleosides evolved to select transfer RNA codon recognition: a modified-wobble hypothesis. Biochimie 73: 1345-1349.
    • (1991) Biochimie , vol.73 , pp. 1345-1349
    • Agris, P.F.1
  • 291
    • 0028069147 scopus 로고
    • Analysis of action of wobble nucleoside modifications on codon-anticodon pairing within the ribosome
    • Lim VI. 1994. Analysis of action of wobble nucleoside modifications on codon-anticodon pairing within the ribosome. J Mol Biol 240: 8-19.
    • (1994) J Mol Biol , vol.240 , pp. 8-19
    • Lim, V.I.1
  • 292
    • 0002365884 scopus 로고
    • Modified nucleosides and codon recognition
    • Söll D and UL Rajbhandary (ed), ASM Press, Washington, D.C
    • Yokoyama S, Nishimura S. 1995. Modified nucleosides and codon recognition, p 207-223. In Söll D and UL Rajbhandary (ed), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 207-223
    • Yokoyama, S.1    Nishimura, S.2
  • 293
    • 0034961959 scopus 로고    scopus 로고
    • Analysis of codon : anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure
    • Lim VI, Curran JF. 2001. Analysis of codon : anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure. RNA 7: 942-957.
    • (2001) RNA , vol.7 , pp. 942-957
    • Lim, V.I.1    Curran, J.F.2
  • 294
    • 0025054368 scopus 로고
    • Codon reading properties of an unmodified transfer RNA
    • Claesson C, Samuelsson T, Lustig F, Borén T. 1990. Codon reading properties of an unmodified transfer RNA. FEBS Lett 273: 173-176.
    • (1990) FEBS Lett , vol.273 , pp. 173-176
    • Claesson, C.1    Samuelsson, T.2    Lustig, F.3    Borén, T.4
  • 295
    • 0015242835 scopus 로고
    • Structure of serine tRNA from Escherichia coli I. Purification of serine tRNA′s with different codon responses.
    • Ishikura H, Yamada Y, Nishimura S. 1971. Structure of serine tRNA from Escherichia coli. I. Purification of serine tRNA′s with different codon responses. Biochim Biophys Acta 228: 471-481.
    • (1971) Biochim Biophys Acta , vol.228 , pp. 471-481
    • Ishikura, H.1    Yamada, Y.2    Nishimura, S.3
  • 296
    • 0018801141 scopus 로고
    • Relative efficiency of anticodons in reading the valine codons during protein synthesis in vitro
    • Mitra SK, Lustig F, Akesson B, Axberg T, Elias P, Lagerkvist U. 1979. Relative efficiency of anticodons in reading the valine codons during protein synthesis in vitro. J Biol Chem 254: 6397-6401.
    • (1979) J Biol Chem , vol.254 , pp. 6397-6401
    • Mitra, S.K.1    Lustig, F.2    Akesson, B.3    Axberg, T.4    Elias, P.5    Lagerkvist, U.6
  • 297
    • 0014683017 scopus 로고
    • Restoration of valine acceptor activity by combining oligonucleotide fragments derived from a Bacillus subtilis ribonuclease digest of Escherichia coli valine transfer RNA
    • Oda K, Kimura F, Harada F, Nishimura S. 1969. Restoration of valine acceptor activity by combining oligonucleotide fragments derived from a Bacillus subtilis ribonuclease digest of Escherichia coli valine transfer RNA. Biochim Biophys Acta 179: 97-105.
    • (1969) Biochim Biophys Acta , vol.179 , pp. 97-105
    • Oda, K.1    Kimura, F.2    Harada, F.3    Nishimura, S.4
  • 299
    • 1242309517 scopus 로고    scopus 로고
    • Decoding the genome: a modified view
    • Agris PF. 2004. Decoding the genome: a modified view. Nucleic Acids Res 32: 223-238.
    • (2004) Nucleic Acids Res , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 300
    • 0032973714 scopus 로고    scopus 로고
    • A single uridine modification at the wobble position of an artificial tRNA enhances wobbling in an Escherichia coli cell-free translation system
    • Takai K, Okumura S, Hosono K, Yokoyama S, Takaku H. 1999. A single uridine modification at the wobble position of an artificial tRNA enhances wobbling in an Escherichia coli cell-free translation system. FEBS Lett 447: 1-4.
    • (1999) FEBS Lett , vol.447 , pp. 1-4
    • Takai, K.1    Okumura, S.2    Hosono, K.3    Yokoyama, S.4    Takaku, H.5
  • 301
  • 302
    • 0030023881 scopus 로고    scopus 로고
    • Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase
    • Gabriel K, Schneider J, McClain WH. 1996. Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase. Science 271: 195-197.
    • (1996) Science , vol.271 , pp. 195-197
    • Gabriel, K.1    Schneider, J.2    McClain, W.H.3
  • 305
    • 0021127317 scopus 로고
    • Undermodification in the first position of the anticodon of supG-tRNA reduces translational efficiency
    • Hagervall TG, Björk GR. 1984. Undermodification in the first position of the anticodon of supG-tRNA reduces translational efficiency. Mol Gen Genet 196: 194-200.
    • (1984) Mol Gen Genet , vol.196 , pp. 194-200
    • Hagervall, T.G.1    Björk, G.R.2
  • 306
    • 0042492708 scopus 로고    scopus 로고
    • The modification of the wobble base of tRNA(Glu) modulates the translation rate of glutamic acid codons in vivo
    • Kruger MK, Pedersen S, Hagervall TG, Sorensen MA. 1998. The modification of the wobble base of tRNA(Glu) modulates the translation rate of glutamic acid codons in vivo. J Mol Biol 284: 621-631.
    • (1998) J Mol Biol , vol.284 , pp. 621-631
    • Kruger, M.K.1    Pedersen, S.2    Hagervall, T.G.3    Sorensen, M.A.4
  • 307
    • 0001409790 scopus 로고
    • Thermodynamic considerations for evolution by RNA
    • Atkins RF Gesterland and JF (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • Turner DH, Bevilacqua PC. 1993. Thermodynamic considerations for evolution by RNA, p 447-464. In Atkins RF Gesterland and JF (ed), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1993) The RNA World , pp. 447-464
    • Turner, D.H.1    Bevilacqua, P.C.2
  • 308
    • 0030839446 scopus 로고    scopus 로고
    • Synthesis and studies on the effect of 2-thiouridine and 4-thiouridine on sugar conformation and RNA duplex stability
    • Kumar RK, Davis DR. 1997. Synthesis and studies on the effect of 2-thiouridine and 4-thiouridine on sugar conformation and RNA duplex stability. Nucleic Acids Res 25: 1272-1280.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1272-1280
    • Kumar, R.K.1    Davis, D.R.2
  • 309
    • 0020611418 scopus 로고
    • NMR analyses on the molecular mechanism of the conformational rigidity of 2-thioribothymidine, a modified nucleoside in extreme thermophile tRNAs
    • Yamamoto Y, Yokoyama S, Miyazawa T, Watanabe K, Higuchi S. 1983. NMR analyses on the molecular mechanism of the conformational rigidity of 2-thioribothymidine, a modified nucleoside in extreme thermophile tRNAs. FEBS Lett 157: 95-99.
    • (1983) FEBS Lett , vol.157 , pp. 95-99
    • Yamamoto, Y.1    Yokoyama, S.2    Miyazawa, T.3    Watanabe, K.4    Higuchi, S.5
  • 310
    • 0019460732 scopus 로고
    • Codon reading and translational error Reading of the glutamine and lysine codons during protein synthesis in vitro
    • Lustig F, Elias P, Axberg T, Samuelsson T, Tittawella I, Lagerkvist U. 1981. Codon reading and translational error. Reading of the glutamine and lysine codons during protein synthesis in vitro. J Biol Chem 256: 2635-2643.
    • (1981) J Biol Chem , vol.256 , pp. 2635-2643
    • Lustig, F.1    Elias, P.2    Axberg, T.3    Samuelsson, T.4    Tittawella, I.5    Lagerkvist, U.6
  • 311
    • 0014682218 scopus 로고
    • Specificity of yeast glutamic acid transfer RNA for codon recognition
    • Sekiya T, Takeishi K, Ukita T. 1969. Specificity of yeast glutamic acid transfer RNA for codon recognition. Biochim Biophys Acta 182: 411-426.
    • (1969) Biochim Biophys Acta , vol.182 , pp. 411-426
    • Sekiya, T.1    Takeishi, K.2    Ukita, T.3
  • 312
    • 0032553438 scopus 로고    scopus 로고
    • Reduced misreading of asparagine codons by Escherichia coli tRNA(Lys) with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position
    • Hagervall TG, Pomerantz SC, McCloskey JA. 1998. Reduced misreading of asparagine codons by Escherichia coli tRNA(Lys) with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position. J Mol Biol 284: 33-42.
    • (1998) J Mol Biol , vol.284 , pp. 33-42
    • Hagervall, T.G.1    Pomerantz, S.C.2    McCloskey, J.A.3
  • 313
    • 0023655732 scopus 로고
    • Missense misreading of asparagine codons as a function of codon identity and context
    • Precup J, Parker J. 1987. Missense misreading of asparagine codons as a function of codon identity and context. J Biol Chem 262: 11351-11355.
    • (1987) J Biol Chem , vol.262 , pp. 11351-11355
    • Precup, J.1    Parker, J.2
  • 314
    • 0029169650 scopus 로고
    • Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA
    • Björk GR. 1995. Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA. Prog Nucleic Acid Res Mol Biol 50: 263-338.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.50 , pp. 263-338
    • Björk, G.R.1
  • 315
    • 0345345078 scopus 로고
    • "Two out of three": an alternative method for codon reading
    • Lagerkvist U. 1978. "Two out of three": an alternative method for codon reading. Proc Natl Acad Sci USA 75: 1759-1762.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 1759-1762
    • Lagerkvist, U.1
  • 316
    • 0030010052 scopus 로고    scopus 로고
    • On the mechanism of leftward frameshifting at several hungry codons
    • Barak Z, Lindsley D, Gallant J. 1996. On the mechanism of leftward frameshifting at several hungry codons. J Mol Biol 256: 676-684.
    • (1996) J Mol Biol , vol.256 , pp. 676-684
    • Barak, Z.1    Lindsley, D.2    Gallant, J.3
  • 317
    • 0343665638 scopus 로고    scopus 로고
    • How translational accuracy influences reading frame maintenance
    • Farabaugh PJ, Björk GR. 1999. How translational accuracy influences reading frame maintenance. EMBO J 18: 1427-1434.
    • (1999) EMBO J , vol.18 , pp. 1427-1434
    • Farabaugh, P.J.1    Björk, G.R.2
  • 318
    • 0026524798 scopus 로고
    • Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group
    • Kawai G, Yamamoto Y, Kamimura T, Masegi T, Sekine M, Hata T, Iimori T, Watanabe T, Miyazawa T, Yokoyama S. 1992. Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group. Biochemistry 31: 1040-1046.
    • (1992) Biochemistry , vol.31 , pp. 1040-1046
    • Kawai, G.1    Yamamoto, Y.2    Kamimura, T.3    Masegi, T.4    Sekine, M.5    Hata, T.6    Iimori, T.7    Watanabe, T.8    Miyazawa, T.9    Yokoyama, S.10
  • 319
    • 0018429379 scopus 로고
    • Specificity of codon recognition by Escherichia coli tRNALeu isoaccepting species determined by protein synthesis in vitro directed by phage RNA
    • Goldman E, Holmes WM, Hatfield GW. 1979. Specificity of codon recognition by Escherichia coli tRNALeu isoaccepting species determined by protein synthesis in vitro directed by phage RNA. J Mol Biol 129: 567-585.
    • (1979) J Mol Biol , vol.129 , pp. 567-585
    • Goldman, E.1    Holmes, W.M.2    Hatfield, G.W.3
  • 320
    • 0032463440 scopus 로고    scopus 로고
    • Novel temperature-sensitive mutants of Escherichia coli that are unable to grow in the absence of wild-type tRNA(6)(Leu)
    • Nakayashiki T, Inokuchi H. 1998. Novel temperature-sensitive mutants of Escherichia coli that are unable to grow in the absence of wild-type tRNA(6)(Leu). J Bacteriol 180: 2931-2935.
    • (1998) J Bacteriol , vol.180 , pp. 2931-2935
    • Nakayashiki, T.1    Inokuchi, H.2
  • 322
    • 0018082458 scopus 로고
    • 4- acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA
    • 4- acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA. J Biol Chem 253: 6132-6139.
    • (1978) J Biol Chem , vol.253 , pp. 6132-6139
    • Stern, L.1    Schulman, L.H.2
  • 323
    • 0015970544 scopus 로고
    • Purification and characterization of AUA specific isoleucine transfer ribonucleic acid from Escherichia coli B
    • Harada F, Nishimura S. 1974. Purification and characterization of AUA specific isoleucine transfer ribonucleic acid from Escherichia coli B. Biochemistry 13: 300-307.
    • (1974) Biochemistry , vol.13 , pp. 300-307
    • Harada, F.1    Nishimura, S.2
  • 325
    • 0019975245 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant lacking tRNA-guanine transglycosylase Function and biosynthesis of queuosine in tRNA.
    • Noguchi S, Nishimura Y, Hirota Y, Nishimura S. 1982. Isolation and characterization of an Escherichia coli mutant lacking tRNA-guanine transglycosylase. Function and biosynthesis of queuosine in tRNA. J Biol Chem 257: 6544-6550.
    • (1982) J Biol Chem , vol.257 , pp. 6544-6550
    • Noguchi, S.1    Nishimura, Y.2    Hirota, Y.3    Nishimura, S.4
  • 327
    • 0037238573 scopus 로고    scopus 로고
    • Putrescine or a combination of methionine and arginine restores virulence gene expression in a tRNA modification-deficient mutant of Shigella flexneri: a possible role in adaptation of virulence
    • Durand JM, Björk GR. 2003. Putrescine or a combination of methionine and arginine restores virulence gene expression in a tRNA modification-deficient mutant of Shigella flexneri: a possible role in adaptation of virulence. Mol Microbiol 47: 519-527.
    • (2003) Mol Microbiol , vol.47 , pp. 519-527
    • Durand, J.M.1    Björk, G.R.2
  • 328
    • 0033965439 scopus 로고    scopus 로고
    • Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: the expression of the virF gene
    • Durand JM, Dagberg B, Uhlin BE, Björk GR. 2000. Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: the expression of the virF gene. Mol Microbiol 35: 924-935.
    • (2000) Mol Microbiol , vol.35 , pp. 924-935
    • Durand, J.M.1    Dagberg, B.2    Uhlin, B.E.3    Björk, G.R.4
  • 329
    • 0028041249 scopus 로고
    • vacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (tgt) of Escherichia coli K-12
    • Durand JM, Okada N, Tobe T, Watarai M, Fukuda I, Suzuki T, Nakata N, Komatsu K, Yoshikawa M, Sasakawa C. 1994. vacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (tgt) of Escherichia coli K-12. J Bacteriol 176: 4627-4634.
    • (1994) J Bacteriol , vol.176 , pp. 4627-4634
    • Durand, J.M.1    Okada, N.2    Tobe, T.3    Watarai, M.4    Fukuda, I.5    Suzuki, T.6    Nakata, N.7    Komatsu, K.8    Yoshikawa, M.9    Sasakawa, C.10
  • 330
    • 0001207805 scopus 로고
    • UAG readthrough during TMV RNA translation: isolation and sequence of two tRNAsTyr with suppressor activity from tobacco plants
    • Beier H, Barciszewska M, Krupp G, Mitnacht R, Gross HJ. 1984. UAG readthrough during TMV RNA translation: isolation and sequence of two tRNAsTyr with suppressor activity from tobacco plants. EMBO J 3: 351-356.
    • (1984) EMBO J , vol.3 , pp. 351-356
    • Beier, H.1    Barciszewska, M.2    Krupp, G.3    Mitnacht, R.4    Gross, H.J.5
  • 332
    • 0024598644 scopus 로고
    • Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr
    • Frey B, Jänel G, Michelsen U, Kersten H. 1989. Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr. J Bacteriol 171: 1524-1530.
    • (1989) J Bacteriol , vol.171 , pp. 1524-1530
    • Frey, B.1    Jänel, G.2    Michelsen, U.3    Kersten, H.4
  • 333
    • 0022036496 scopus 로고
    • Queuosine modification of the wobble base in tRNAHis influences 'in vivo' decoding properties
    • Meier F, Suter B, Grosjean H, Keith G, Kubli E. 1985. Queuosine modification of the wobble base in tRNAHis influences 'in vivo' decoding properties. EMBO J 4: 823-827.
    • (1985) EMBO J , vol.4 , pp. 823-827
    • Meier, F.1    Suter, B.2    Grosjean, H.3    Keith, G.4    Kubli, E.5
  • 334
    • 0035028632 scopus 로고    scopus 로고
    • An extended structural signature for the tRNA anticodon loop
    • Auffinger P, Westhof E. 2001. An extended structural signature for the tRNA anticodon loop. RNA 7: 334-341.
    • (2001) RNA , vol.7 , pp. 334-341
    • Auffinger, P.1    Westhof, E.2
  • 336
    • 0036303671 scopus 로고    scopus 로고
    • Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe)
    • Cabello-Villegas J, Winkler ME, Nikonowicz EP. 2002. Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe). J Mol Biol 319: 1015-1034.
    • (2002) J Mol Biol , vol.319 , pp. 1015-1034
    • Cabello-Villegas, J.1    Winkler, M.E.2    Nikonowicz, E.P.3
  • 337
    • 0345304724 scopus 로고    scopus 로고
    • Naturally- occurring Modification Restricts the Anticodon Domain Conformational Space of tRNA(Phe)
    • Stuart JW, Koshlap KM, Guenther R, Agris PF. 2003. Naturally- occurring Modification Restricts the Anticodon Domain Conformational Space of tRNA(Phe). J Mol Biol 334: 901-918.
    • (2003) J Mol Biol , vol.334 , pp. 901-918
    • Stuart, J.W.1    Koshlap, K.M.2    Guenther, R.3    Agris, P.F.4
  • 338
    • 0017064254 scopus 로고
    • The involvement of the anticodon adjacent modified nucleoside N-(9-(β-D-ribofuranosyl) purine-6-ylcarbamoyl)-threonine in the biological function of E coli tRNAile.
    • Miller JP, Hussain Z, Schweizer MP. 1976. The involvement of the anticodon adjacent modified nucleoside N-(9-(β-D-ribofuranosyl) purine-6-ylcarbamoyl)-threonine in the biological function of E. coli tRNAile. Nucleic Acids Res 3: 1185-1201.
    • (1976) Nucleic Acids Res , vol.3 , pp. 1185-1201
    • Miller, J.P.1    Hussain, Z.2    Schweizer, M.P.3
  • 340
    • 0026357506 scopus 로고
    • 6A deficiency enhances proofreading in translation
    • 6A deficiency enhances proofreading in translation. J Mol Biol 222: 1161-1171.
    • (1991) J Mol Biol , vol.222 , pp. 1161-1171
    • Diaz, I.1    Ehrenberg, M.2
  • 341
    • 0021710557 scopus 로고
    • The effect of point mutations affecting Escherichia coli tryptophan tRNA on anticodon-anticodon interactions and on UGA suppression
    • Vacher J, Grosjean H, Houssier C, Buckingham RH. 1984. The effect of point mutations affecting Escherichia coli tryptophan tRNA on anticodon-anticodon interactions and on UGA suppression. J Mol Biol 177: 329-342.
    • (1984) J Mol Biol , vol.177 , pp. 329-342
    • Vacher, J.1    Grosjean, H.2    Houssier, C.3    Buckingham, R.H.4
  • 342
    • 0027165203 scopus 로고
    • 6A37 in tRNA, mutation in rpsD (S4) or streptomycin.
    • 6A37 in tRNA, mutation in rpsD (S4) or streptomycin. J Mol Biol 232: 1017-1029.
    • (1993) J Mol Biol , vol.232 , pp. 1017-1029
    • Björnsson, A.1    Isaksson, L.A.2
  • 343
    • 0022656871 scopus 로고
    • Influence of modification next to the anticodon in tRNA on codon context sensitivity of translational suppression and accuracy
    • Bouadloun F, Srichaiyo T, Isaksson LA, Björk GR. 1986. Influence of modification next to the anticodon in tRNA on codon context sensitivity of translational suppression and accuracy. J Bacteriol 166: 1022-1027.
    • (1986) J Bacteriol , vol.166 , pp. 1022-1027
    • Bouadloun, F.1    Srichaiyo, T.2    Isaksson, L.A.3    Björk, G.R.4
  • 344
    • 0025822316 scopus 로고
    • 6-(4-hydroxyisopentenyl)adenosine distinguish between bases 3′ of the codon
    • 6-(4-hydroxyisopentenyl)adenosine distinguish between bases 3′ of the codon. J Mol Biol 218: 509-516.
    • (1991) J Mol Biol , vol.218 , pp. 509-516
    • Ericson, J.U.1    Björk, G.R.2
  • 345
    • 0020511286 scopus 로고
    • The role of 2-methylthio-N6-isopentenyladenosine in readthrough and suppression of nonsense codons in Escherichia coli
    • Petrullo LA, Gallagher PJ, Elseviers D. 1983. The role of 2-methylthio-N6-isopentenyladenosine in readthrough and suppression of nonsense codons in Escherichia coli. Mol Gen Genet 190: 289-294.
    • (1983) Mol Gen Genet , vol.190 , pp. 289-294
    • Petrullo, L.A.1    Gallagher, P.J.2    Elseviers, D.3
  • 346
    • 0020489739 scopus 로고
    • Iron mediated methylthiolation of tRNA as a regulator of operon expression in Escherichia coli
    • Buck M, Griffiths E. 1982. Iron mediated methylthiolation of tRNA as a regulator of operon expression in Escherichia coli. Nucleic Acids Res 10: 2609-2624.
    • (1982) Nucleic Acids Res , vol.10 , pp. 2609-2624
    • Buck, M.1    Griffiths, E.2
  • 347
    • 0023369964 scopus 로고
    • Effects of miaA on translation and growth rates
    • Diaz I, Pedersen S, Kurland CG. 1987. Effects of miaA on translation and growth rates. Mol Gen Genet 208: 373-376.
    • (1987) Mol Gen Genet , vol.208 , pp. 373-376
    • Diaz, I.1    Pedersen, S.2    Kurland, C.G.3
  • 348
    • 0024261115 scopus 로고
    • Media dependence of translational mutant phenotype
    • Mikkola R, Kurland CG. 1988. Media dependence of translational mutant phenotype. FEMS Microbiol Lett 56: 265-270.
    • (1988) FEMS Microbiol Lett , vol.56 , pp. 265-270
    • Mikkola, R.1    Kurland, C.G.2
  • 349
    • 0037310284 scopus 로고    scopus 로고
    • 1-Methylguanosine-deficient tRNA of Salmonella enterica serovar Typhimurium affects thiamine metabolism
    • Björk GR, Nilsson K. 2003. 1-Methylguanosine-deficient tRNA of Salmonella enterica serovar Typhimurium affects thiamine metabolism. J Bacteriol 185: 750-759.
    • (2003) J Bacteriol , vol.185 , pp. 750-759
    • Björk, G.R.1    Nilsson, K.2
  • 350
    • 0029619250 scopus 로고
    • Functional analysis of the ffh-trmD region of the Escherichia coli chromosome by using reverse genetics
    • Persson BC, Bylund GO, Berg DE, Wikström PM. 1995. Functional analysis of the ffh-trmD region of the Escherichia coli chromosome by using reverse genetics. J Bacteriol 177: 5554-5560.
    • (1995) J Bacteriol , vol.177 , pp. 5554-5560
    • Persson, B.C.1    Bylund, G.O.2    Berg, D.E.3    Wikström, P.M.4
  • 352
    • 0028832208 scopus 로고
    • 1-methylguanosine deficiency of tRNA influences cognate codon interaction and metabolism in Salmonella typhimurium
    • Li JN, Björk GR. 1995. 1-methylguanosine deficiency of tRNA influences cognate codon interaction and metabolism in Salmonella typhimurium. J Bacteriol 177: 6593-6600.
    • (1995) J Bacteriol , vol.177 , pp. 6593-6600
    • Li, J.N.1    Björk, G.R.2
  • 353
    • 0020531026 scopus 로고
    • Effects of the hisT mutation of Salmonella typhimurium on translation elongation rate
    • Palmer DT, Blum PH, Artz SW. 1983. Effects of the hisT mutation of Salmonella typhimurium on translation elongation rate. J Bacteriol 153: 357-363.
    • (1983) J Bacteriol , vol.153 , pp. 357-363
    • Palmer, D.T.1    Blum, P.H.2    Artz, S.W.3
  • 354
    • 0019308408 scopus 로고
    • The influence of codon context on genetic code translation
    • Bossi L, Roth JR. 1980. The influence of codon context on genetic code translation. Nature 286: 123-127.
    • (1980) Nature , vol.286 , pp. 123-127
    • Bossi, L.1    Roth, J.R.2
  • 356
    • 0020450422 scopus 로고
    • Specific mistranslation in hisT mutants of Escherichia coli
    • Parker J. 1982. Specific mistranslation in hisT mutants of Escherichia coli. Mol Gen Genet 187: 405-409.
    • (1982) Mol Gen Genet , vol.187 , pp. 405-409
    • Parker, J.1
  • 357
    • 0025922011 scopus 로고
    • Phe from hisT mutants: a structural role for pseudouridine
    • Phe from hisT mutants: a structural role for pseudouridine. Biochemistry 30: 4223-4231.
    • (1991) Biochemistry , vol.30 , pp. 4223-4231
    • Davis, D.R.1    Poulter, C.D.2
  • 358
    • 0033534387 scopus 로고    scopus 로고
    • Stabilization of the anticodon stem-loop of tRNA(LyS,3) by an A(+)-C base-pair and by pseudouridine
    • Durant PC, Davis DR. 1999. Stabilization of the anticodon stem-loop of tRNA(LyS,3) by an A(+)-C base-pair and by pseudouridine. J Mol Biol 285: 115-131.
    • (1999) J Mol Biol , vol.285 , pp. 115-131
    • Durant, P.C.1    Davis, D.R.2
  • 359
    • 0019250651 scopus 로고
    • 4-Thiouridine triggers both growth delay induced by near-ultraviolet light and photoprotection
    • Thomas G, Favre A. 1980. 4-Thiouridine triggers both growth delay induced by near-ultraviolet light and photoprotection. Eur J Biochem 113: 67-74.
    • (1980) Eur J Biochem , vol.113 , pp. 67-74
    • Thomas, G.1    Favre, A.2
  • 360
    • 0018462013 scopus 로고
    • Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance
    • Davanloo P, Sprinzl M, Watanabe K, Albani M, Kersten H. 1979. Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance. Nucleic Acids Res 6: 1571-1581.
    • (1979) Nucleic Acids Res , vol.6 , pp. 1571-1581
    • Davanloo, P.1    Sprinzl, M.2    Watanabe, K.3    Albani, M.4    Kersten, H.5
  • 362
    • 0036855267 scopus 로고    scopus 로고
    • Physiological analysis of the role of truB in Escherichia coli: a role for tRNA modification in extreme temperature resistance
    • Kinghorn SM, O'Byrne CP, Booth IR, Stansfield I. 2002. Physiological analysis of the role of truB in Escherichia coli: a role for tRNA modification in extreme temperature resistance. Microbiology 148: 3511-3520.
    • (2002) Microbiology , vol.148 , pp. 3511-3520
    • Kinghorn, S.M.1    O'Byrne, C.P.2    Booth, I.R.3    Stansfield, I.4
  • 363
    • 0036776779 scopus 로고    scopus 로고
    • Three modifications in the D and T arms of tRNA influence translation in Escherichia coli and expression of virulence genes in Shigella flexneri
    • Urbonavicius J, Durand JM, Björk GR. 2002. Three modifications in the D and T arms of tRNA influence translation in Escherichia coli and expression of virulence genes in Shigella flexneri. J Bacteriol 184: 5348-5357.
    • (2002) J Bacteriol , vol.184 , pp. 5348-5357
    • Urbonavicius, J.1    Durand, J.M.2    Björk, G.R.3
  • 366
    • 0014423983 scopus 로고
    • Nucleotide sequence of N-formyl-methionyl-transfer RNA
    • Dube SK, Marcker KA, Clark BF, Cory S. 1968. Nucleotide sequence of N-formyl-methionyl-transfer RNA. Nature 218: 232-233.
    • (1968) Nature , vol.218 , pp. 232-233
    • Dube, S.K.1    Marcker, K.A.2    Clark, B.F.3    Cory, S.4
  • 367
    • 0015912658 scopus 로고
    • Possibilities for the evolution of the genetic code from a preceding form
    • Jukes TH. 1973. Possibilities for the evolution of the genetic code from a preceding form. Nature 246: 22-26.
    • (1973) Nature , vol.246 , pp. 22-26
    • Jukes, T.H.1
  • 368
    • 0015278178 scopus 로고
    • Minor components in transfer RNA: their characterization, location, and function
    • Nishimura S. 1972. Minor components in transfer RNA: their characterization, location, and function. Prog Nucl Acid Res Mol Biol 12: 49-85.
    • (1972) Prog Nucl Acid Res Mol Biol , vol.12 , pp. 49-85
    • Nishimura, S.1
  • 369
    • 0000190405 scopus 로고    scopus 로고
    • Limitations of translation accuracy
    • Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Cellular and Molecular Biology. ASM Press, Washington, D.C
    • Kurland CG, Hughes D, Ehrenberg M. 1996. Limitations of translation accuracy, p 979-1004. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella. Cellular and Molecular Biology. ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella , pp. 979-1004
    • Kurland, C.G.1    Hughes, D.2    Ehrenberg, M.3
  • 370
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Björk GR. 2001. Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J 20: 4863-4873.
    • (2001) EMBO J , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Björk, G.R.5
  • 372
    • 0029073174 scopus 로고
    • Prokaryotic ribosomes recode the HIV-1 gag-pol-1 frameshift sequence by an E/P site post-translocation simultaneous slippage mechanism
    • Horsfield JA, Wilson DN, Mannering SA, Adamski FM, Tate WP. 1995. Prokaryotic ribosomes recode the HIV-1 gag-pol-1 frameshift sequence by an E/P site post-translocation simultaneous slippage mechanism. Nucleic Acids Res 23: 1487-1494.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1487-1494
    • Horsfield, J.A.1    Wilson, D.N.2    Mannering, S.A.3    Adamski, F.M.4    Tate, W.P.5
  • 373
    • 0036534459 scopus 로고    scopus 로고
    • Ribosome structure:revisiting the connection between translational accuracy and unconventional decoding
    • Stahl G, McCarty GP, Farabaugh PJ. 2002. Ribosome structure:revisiting the connection between translational accuracy and unconventional decoding. Trends Biochem Sci 27: 178-183.
    • (2002) Trends Biochem Sci , vol.27 , pp. 178-183
    • Stahl, G.1    McCarty, G.P.2    Farabaugh, P.J.3
  • 375
    • 0025303605 scopus 로고
    • Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site
    • Belcourt MF, Farabaugh PJ. 1990. Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site. Cell 62: 339-352.
    • (1990) Cell , vol.62 , pp. 339-352
    • Belcourt, M.F.1    Farabaugh, P.J.2
  • 376
    • 0024316220 scopus 로고
    • Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine
    • Björk GR, Wikström PM, Byström AS. 1989. Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine. Science 244: 986-989.
    • (1989) Science , vol.244 , pp. 986-989
    • Björk, G.R.1    Wikström, P.M.2    Byström, A.S.3
  • 377
    • 0031567788 scopus 로고    scopus 로고
    • ProGGG of Salmonella typhimurium induce +1 frameshifting at the peptidyl-site
    • ProGGG of Salmonella typhimurium induce +1 frameshifting at the peptidyl-site. J Mol Biol 273: 978-992.
    • (1997) J Mol Biol , vol.273 , pp. 978-992
    • Qian, Q.1    Björk, G.R.2
  • 379
    • 0141625262 scopus 로고    scopus 로고
    • Programmed translational -1 frameshifting on hexanucleotide motifs and the wobble properties of tRNAs
    • Licznar P, Mejlhede N, Prère MF, Wills N, Gesteland RF, Atkins JF, Fayet O. 2003. Programmed translational -1 frameshifting on hexanucleotide motifs and the wobble properties of tRNAs. EMBO J 22: 4770-4778.
    • (2003) EMBO J , vol.22 , pp. 4770-4778
    • Licznar, P.1    Mejlhede, N.2    Prère, M.F.3    Wills, N.4    Gesteland, R.F.5    Atkins, J.F.6    Fayet, O.7
  • 380
    • 0031577333 scopus 로고    scopus 로고
    • Expression of a coronavirus ribosomal frameshift signal in Escherichia coli: influence of tRNA anticodon modification on frameshifting
    • Brierley I, Meredith MR, Bloys AJ, Hagervall TG. 1997. Expression of a coronavirus ribosomal frameshift signal in Escherichia coli: influence of tRNA anticodon modification on frameshifting. J Mol Biol 270: 360-373.
    • (1997) J Mol Biol , vol.270 , pp. 360-373
    • Brierley, I.1    Meredith, M.R.2    Bloys, A.J.3    Hagervall, T.G.4
  • 382
    • 0016587458 scopus 로고
    • Unbalanced growth and the production of unique transfer ribonucleic acids in relaxed-control Escherichia coli
    • Kitchingman GR, Fournier MJ. 1975. Unbalanced growth and the production of unique transfer ribonucleic acids in relaxed-control Escherichia coli. J Bacteriol 124: 1382-1394.
    • (1975) J Bacteriol , vol.124 , pp. 1382-1394
    • Kitchingman, G.R.1    Fournier, M.J.2
  • 383
    • 0017691755 scopus 로고
    • Modification-deficient transfer ribonucleic acids from relaxed control Escherichia coli:structures of the major undermodified phenylalanine and leucine transfer RNAs produced during leucine starvation
    • Kitchingman GR, Fournier MJ. 1977. Modification-deficient transfer ribonucleic acids from relaxed control Escherichia coli:structures of the major undermodified phenylalanine and leucine transfer RNAs produced during leucine starvation. Biochemistry 16: 2213-2220.
    • (1977) Biochemistry , vol.16 , pp. 2213-2220
    • Kitchingman, G.R.1    Fournier, M.J.2
  • 384
    • 0017134133 scopus 로고
    • Unique phenylalanine transfer ribonucleic acids in relaxed control Escherichia coli: genetic origin and some functional properties
    • Kitchingman GR, Webb E, Fournier MJ. 1976. Unique phenylalanine transfer ribonucleic acids in relaxed control Escherichia coli: genetic origin and some functional properties. Biochemistry 15: 1848-1857.
    • (1976) Biochemistry , vol.15 , pp. 1848-1857
    • Kitchingman, G.R.1    Webb, E.2    Fournier, M.J.3
  • 385
    • 0017886450 scopus 로고
    • Alteration of the intracellular concentration of aminoacyl-tRNA synthetases and isoaccepting tRNAs during amino-acid limited growth in Escherichia coli
    • Thomale J, Nass G. 1978. Alteration of the intracellular concentration of aminoacyl-tRNA synthetases and isoaccepting tRNAs during amino-acid limited growth in Escherichia coli. Eur J Biochem 85: 407-418.
    • (1978) Eur J Biochem , vol.85 , pp. 407-418
    • Thomale, J.1    Nass, G.2
  • 386
    • 0014873757 scopus 로고
    • Identification of the cytokinin-active ribonucleosides in pure Escherichia coli tRNA species
    • Bartz J, Söll D, Burrows WJ, Skoog F. 1970. Identification of the cytokinin-active ribonucleosides in pure Escherichia coli tRNA species. Proc Natl Acad Sci USA 67: 1448-1453.
    • (1970) Proc Natl Acad Sci USA , vol.67 , pp. 1448-1453
    • Bartz, J.1    Söll, D.2    Burrows, W.J.3    Skoog, F.4
  • 389
    • 0018165537 scopus 로고
    • Alterations in the tRNA′s of Escherichia coli recovered from lethally infected animals
    • Griffiths E, Humphreys J, Leach A, Scanlon L. 1978. Alterations in the tRNA′s of Escherichia coli recovered from lethally infected animals. Infect Immun 22: 312-317.
    • (1978) Infect Immun , vol.22 , pp. 312-317
    • Griffiths, E.1    Humphreys, J.2    Leach, A.3    Scanlon, L.4
  • 390
    • 0013240174 scopus 로고
    • Physiological effects of near-ultraviolet radiation on bacteria
    • Jagger J. 1983. Physiological effects of near-ultraviolet radiation on bacteria. Photochem Photobiol Rev 7: 1-73.
    • (1983) Photochem Photobiol Rev , vol.7 , pp. 1-73
    • Jagger, J.1
  • 391
    • 0023879618 scopus 로고
    • Near-UV stress in Salmonella typhimurium: 4-thiouridine in tRNA, ppGpp, and ApppGpp as components of an adaptive response
    • Kramer GF, Baker JC, Ames BN. 1988. Near-UV stress in Salmonella typhimurium: 4-thiouridine in tRNA, ppGpp, and ApppGpp as components of an adaptive response. J Bacteriol 170: 2344-2351.
    • (1988) J Bacteriol , vol.170 , pp. 2344-2351
    • Kramer, G.F.1    Baker, J.C.2    Ames, B.N.3
  • 392
    • 2642704382 scopus 로고
    • Mechanism of growth delay induced in Escherichia coli by near ultraviolet radiation
    • Ramabhadran TV, Jagger J. 1976. Mechanism of growth delay induced in Escherichia coli by near ultraviolet radiation. Proc Natl Acad Sci USA 73: 59-63.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 59-63
    • Ramabhadran, T.V.1    Jagger, J.2
  • 393
    • 0019800629 scopus 로고
    • tRNA thiolated pyrimidines as targets for near-ultraviolet-induced synthesis of guanosine tetraphosphate in Escherichia coli
    • Thomas G, Thiam K, Favre A. 1981. tRNA thiolated pyrimidines as targets for near-ultraviolet-induced synthesis of guanosine tetraphosphate in Escherichia coli. Eur J Biochem 119: 381-387.
    • (1981) Eur J Biochem , vol.119 , pp. 381-387
    • Thomas, G.1    Thiam, K.2    Favre, A.3
  • 395
    • 0016701053 scopus 로고
    • 4-Thiouridine as the target for nearultraviolet light induced growth delay in Escherichia coli
    • Thomas G, Favre A. 1975. 4-Thiouridine as the target for nearultraviolet light induced growth delay in Escherichia coli. Biochem Biophys Res Commun 66: 1454-1461.
    • (1975) Biochem Biophys Res Commun , vol.66 , pp. 1454-1461
    • Thomas, G.1    Favre, A.2
  • 396
    • 0021867941 scopus 로고
    • Mutagenesis and growth delay induced in Escherichia coli by nearultraviolet radiations
    • Favre A, Hajnsdorf E, Thiam K, Caldeira de Araujo A. 1985. Mutagenesis and growth delay induced in Escherichia coli by nearultraviolet radiations. Biochimie 67: 335-342.
    • (1985) Biochimie , vol.67 , pp. 335-342
    • Favre, A.1    Hajnsdorf, E.2    Thiam, K.3    Caldeira de Araujo, A.4
  • 397
    • 0022612135 scopus 로고
    • Near ultraviolet DNA damage induces the SOS responses in Escherichia coli
    • Caldeira de Araujo A, Favre A. 1986. Near ultraviolet DNA damage induces the SOS responses in Escherichia coli. EMBO J 5: 175-179.
    • (1986) EMBO J , vol.5 , pp. 175-179
    • Caldeira de Araujo, A.1    Favre, A.2
  • 398
    • 0021276634 scopus 로고
    • Salmonella typhimurium synthesizes cobalamin (vitamin B12) de novo under anaerobic growth conditions
    • Jeter RM, Olivera BM, Roth JR. 1984. Salmonella typhimurium synthesizes cobalamin (vitamin B12) de novo under anaerobic growth conditions. J Bacteriol 159: 206-213.
    • (1984) J Bacteriol , vol.159 , pp. 206-213
    • Jeter, R.M.1    Olivera, B.M.2    Roth, J.R.3
  • 399
    • 0017800273 scopus 로고
    • Lys on the regulation of lysine biosynthesis in Escherichia coli
    • Lys on the regulation of lysine biosynthesis in Escherichia coli. Mol Gen Genet 159: 33-38.
    • (1978) Mol Gen Genet , vol.159 , pp. 33-38
    • Boy, E.1    Borne, F.2    Patte, J.C.3
  • 400
    • 84908751192 scopus 로고
    • Transfer RNA involvment in the regulation of enzyme synthesis
    • Brenchley JE, Williams LS. 1975. Transfer RNA involvment in the regulation of enzyme synthesis. Annu Rev Microbiol 29: 251-274.
    • (1975) Annu Rev Microbiol , vol.29 , pp. 251-274
    • Brenchley, J.E.1    Williams, L.S.2
  • 401
    • 0016190222 scopus 로고
    • Pleiotropy of hisT mutants blocked in pseudouridine synthesis in tRNA: leucine and isoleucine-valine operons
    • Cortese R, Landsberg R, Haar RA, Umbarger HE, Ames BN. 1974. Pleiotropy of hisT mutants blocked in pseudouridine synthesis in tRNA: leucine and isoleucine-valine operons. Proc Natl Acad Sci USA 71: 1857-1861.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1857-1861
    • Cortese, R.1    Landsberg, R.2    Haar, R.A.3    Umbarger, H.E.4    Ames, B.N.5
  • 402
    • 0018366240 scopus 로고
    • Pseudouridylation of tRNAs and its role in regulation in Salmonella typhimurium
    • Turnbough CL Jr, Neill RJ, Landsberg R, Ames BN. 1979. Pseudouridylation of tRNAs and its role in regulation in Salmonella typhimurium. J Biol Chem 254: 5111-5119.
    • (1979) J Biol Chem , vol.254 , pp. 5111-5119
    • Turnbough, C.L.1    Neill, R.J.2    Landsberg, R.3    Ames, B.N.4
  • 404
    • 0024565639 scopus 로고
    • Relationship between guanosine tetraphosphate and accuracy of translation in Salmonella typhimurium
    • Nègre D, Cortay JC, Donini P, Cozzone AJ. 1989. Relationship between guanosine tetraphosphate and accuracy of translation in Salmonella typhimurium. Biochemistry 28: 1814-1819.
    • (1989) Biochemistry , vol.28 , pp. 1814-1819
    • Nègre, D.1    Cortay, J.C.2    Donini, P.3    Cozzone, A.J.4
  • 405
    • 0016604910 scopus 로고
    • Reduced maximal levels of derepression of the isoleucine-valine and leucine enzymes in hisT mutants of Salmonella typhimurium
    • Bresalier RS, Rizzino AA, Freundlich M. 1975. Reduced maximal levels of derepression of the isoleucine-valine and leucine enzymes in hisT mutants of Salmonella typhimurium. Nature 253: 279-280.
    • (1975) Nature , vol.253 , pp. 279-280
    • Bresalier, R.S.1    Rizzino, A.A.2    Freundlich, M.3
  • 406
    • 0002958061 scopus 로고    scopus 로고
    • Links between tRNA modification and metabolism and modified nucleosides as tumor marker
    • Grosjean H and Benne B (ed), ASM Press, Washington, D.C
    • Björk GR, Rasmuson T. 1998. Links between tRNA modification and metabolism and modified nucleosides as tumor marker, p 471-491. In Grosjean H and Benne B (ed), Modification and Editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 471-491
    • Björk, G.R.1    Rasmuson, T.2
  • 407
    • 1842376275 scopus 로고    scopus 로고
    • The modified nucleoside 2-methylthio-N-6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes
    • Durand JMB, Björk GR, Kuwae A, Yoshikawa M, Sasakawa C. 1997. The modified nucleoside 2-methylthio-N-6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes. J Bacteriol 179: 5777-5782.
    • (1997) J Bacteriol , vol.179 , pp. 5777-5782
    • Durand, J.M.B.1    Björk, G.R.2    Kuwae, A.3    Yoshikawa, M.4    Sasakawa, C.5
  • 408
    • 0842283048 scopus 로고    scopus 로고
    • Molecular characterization of a glucoseinhibited division gene, gidA, that regulates cytotoxic enterotoxin of Aeromonas hydrophila
    • Sha J, Kozlova EV, Fadl AA, Olano JP, Houston CW, Peterson JW, Chopra AK. 2004. Molecular characterization of a glucoseinhibited division gene, gidA, that regulates cytotoxic enterotoxin of Aeromonas hydrophila. Infect Immun 72: 1084-1095.
    • (2004) Infect Immun , vol.72 , pp. 1084-1095
    • Sha, J.1    Kozlova, E.V.2    Fadl, A.A.3    Olano, J.P.4    Houston, C.W.5    Peterson, J.W.6    Chopra, A.K.7
  • 409
    • 0036202217 scopus 로고    scopus 로고
    • Global regulation by gidA in Pseudomonas syringae
    • Kinscherf TG, Willis DK. 2002. Global regulation by gidA in Pseudomonas syringae. J Bacteriol 184: 2281-2286.
    • (2002) J Bacteriol , vol.184 , pp. 2281-2286
    • Kinscherf, T.G.1    Willis, D.K.2
  • 410
    • 0026574201 scopus 로고
    • Evidence for a new, oxygen-regulated biosynthetic pathway for the pyrimidine moiety of thiamine in Salmonella typhimurium
    • Downs DM. 1992. Evidence for a new, oxygen-regulated biosynthetic pathway for the pyrimidine moiety of thiamine in Salmonella typhimurium. J Bacteriol 174: 1515-1521.
    • (1992) J Bacteriol , vol.174 , pp. 1515-1521
    • Downs, D.M.1
  • 411
    • 0026047677 scopus 로고
    • Synthesis of thiamine in Salmonella typhimurium independent of the purF function
    • Downs DM, Roth JR. 1991. Synthesis of thiamine in Salmonella typhimurium independent of the purF function. J Bacteriol 173: 6597-6604.
    • (1991) J Bacteriol , vol.173 , pp. 6597-6604
    • Downs, D.M.1    Roth, J.R.2
  • 412
    • 0028144751 scopus 로고
    • apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella typhimurium
    • Downs DM, Petersen L. 1994. apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella typhimurium. J Bacteriol 176: 4858-4864.
    • (1994) J Bacteriol , vol.176 , pp. 4858-4864
    • Downs, D.M.1    Petersen, L.2
  • 413
    • 0018949228 scopus 로고
    • Regulation of nitrogen utilization of hisT mutants of Salmonella typhimurium
    • Rosenfeld SA, Brenchley JE. 1980. Regulation of nitrogen utilization of hisT mutants of Salmonella typhimurium. J Bacteriol 143: 801-808.
    • (1980) J Bacteriol , vol.143 , pp. 801-808
    • Rosenfeld, S.A.1    Brenchley, J.E.2
  • 414
    • 0017858420 scopus 로고
    • Branched-chain amino acid transport regulation in mutants blocked in tRNA maturation and transcriptional termination
    • Quay SC, Lawther RP, Hatfield GW, Oxender DL. 1978. Branched-chain amino acid transport regulation in mutants blocked in tRNA maturation and transcriptional termination. J Bacteriol 134: 683-686.
    • (1978) J Bacteriol , vol.134 , pp. 683-686
    • Quay, S.C.1    Lawther, R.P.2    Hatfield, G.W.3    Oxender, D.L.4
  • 415
    • 0025213112 scopus 로고
    • Altered growth-ratedependent regulation of 6-phosphogluconate dehydrogenase level in hisT mutants of Salmonella typhimurium and Escherichia coli
    • Jones WR, Barcak GJ, Wolf RE, Jr. 1990. Altered growth-ratedependent regulation of 6-phosphogluconate dehydrogenase level in hisT mutants of Salmonella typhimurium and Escherichia coli. J Bacteriol 172: 1197-1205.
    • (1990) J Bacteriol , vol.172 , pp. 1197-1205
    • Jones, W.R.1    Barcak, G.J.2    Wolf, R.E.3
  • 416
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • Tsui HCT, Leung HCE, Winkler ME. 1994. Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol Microbiol 13: 35-49.
    • (1994) Mol Microbiol , vol.13 , pp. 35-49
    • Tsui, H.C.T.1    Leung, H.C.E.2    Winkler, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.