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Volumn 5, Issue 3, 1999, Pages 395-408

Structural alterations of the tRNA(m1G37)methyltransferase from Salmonella typhimurium affect tRNA substrate specificity

Author keywords

1 methylguanosine; Modification; Recognition

Indexed keywords

GENE PRODUCT; TRANSFER RNA;

EID: 0344923796     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838299980834     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 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
  • 2
    • 0002495140 scopus 로고
    • Biosynthesis and function of modified nucleosides in tRNA
    • Söll D, RajBhandary UL, eds. Washington, DC: ASM Press
    • Björk GR. 1995. Biosynthesis and function of modified nucleosides in tRNA. In: Söll D, RajBhandary UL, eds. tRNA: Structure, biosynthesis, and function. Washington, DC: ASM Press. pp 165-205.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 165-205
    • Björk, G.R.1
  • 3
    • 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
  • 4
    • 0021103441 scopus 로고
    • Complete analysis of tRNA-modified nucleosides by high-performance liquid chromatography: The 29 modified nucleosides of Salmonella typhimurium and Escherichia coli tRNA
    • Buck M, Connick M, Ames BN. 1983. Complete analysis of tRNA-modified nucleosides by high-performance liquid chromatography: The 29 modified nucleosides of Salmonella typhimurium and Escherichia coli tRNA. Anal Biochem 129:1-13.
    • (1983) Anal Biochem , vol.129 , pp. 1-13
    • Buck, M.1    Connick, M.2    Ames, B.N.3
  • 5
    • 0002596822 scopus 로고    scopus 로고
    • Modified nucleosides always were: An evolutionary model
    • Grosjean H, Benne R, eds. Washington, DC: ASM Press
    • Cermakian N, Cedergren R. 1998. Modified nucleosides always were: An evolutionary model. In: Grosjean H, Benne R, eds. Modification and editing of RNA. Washington, DC: ASM Press. pp 535-541.
    • (1998) Modification and Editing of RNA , pp. 535-541
    • Cermakian, N.1    Cedergren, R.2
  • 6
    • 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
  • 8
    • 0022719475 scopus 로고
    • Enzymatic 2′-O-methylation of the wobble nucleoside of eukaryotic tRNAPhe: Specificity depends on structural elements outside the anticodon loop
    • Droogmans L, Haumont E, de Henau S, Grosjean H. 1986. Enzymatic 2′-O-methylation of the wobble nucleoside of eukaryotic tRNAPhe: Specificity depends on structural elements outside the anticodon loop. EMBO J 5:1105-1109.
    • (1986) EMBO J , vol.5 , pp. 1105-1109
    • Droogmans, L.1    Haumont, E.2    De Henau, S.3    Grosjean, H.4
  • 9
    • 0027935988 scopus 로고
    • Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme
    • Edqvist J, Blomqvist K, Stråby KB. 1994. Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme. Biochemistry 33:9546-9551.
    • (1994) Biochemistry , vol.33 , pp. 9546-9551
    • Edqvist, J.1    Blomqvist, K.2    Stråby, K.B.3
  • 11
    • 0019935329 scopus 로고
    • Quantitative enzymatic hydrolysis of tRNAs: Reversed-phase high-performance liquid chromatography of tRNA nucleosides
    • Gehrke CW, Kuo KC, McCune RA, Gerhardt KO, Agris PF. 1982. Quantitative enzymatic hydrolysis of tRNAs: Reversed-phase high-performance liquid chromatography of tRNA nucleosides. J Chromatogr A 230:297-308.
    • (1982) J Chromatogr A , vol.230 , pp. 297-308
    • Gehrke, C.W.1    Kuo, K.C.2    McCune, R.A.3    Gerhardt, K.O.4    Agris, P.F.5
  • 12
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • Grosjean H, Edqvist J, Stråby KB, Giegé R. 1996. Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture. J Mol Biol 255:67-85.
    • (1996) J Mol Biol , vol.255 , pp. 67-85
    • Grosjean, H.1    Edqvist, J.2    Stråby, K.B.3    Giegé, R.4
  • 13
    • 0029786633 scopus 로고    scopus 로고
    • Recognition of the T-arm of tRNA by tRNA (m(5) U54)-methyltransferase is not sequence specific
    • Gu XR, Ivanetich KM, Santi DV. 1996. Recognition of the T-arm 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
  • 14
    • 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
  • 15
    • 0015187451 scopus 로고
    • Localized mutagenesis of any specific small region of the bacterial chromosome
    • Hong JS, Ames BN. 1971. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc Natl Acad Sci USA 68:3158-3162.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 3158-3162
    • Hong, J.S.1    Ames, B.N.2
  • 16
    • 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
  • 17
    • 0022422726 scopus 로고
    • Structure and transcription of the tRNAPro1 gene from Escherichia coli
    • Kuchino Y, Mori F, Nishimura S. 1985. Structure and transcription of the tRNAPro1 gene from Escherichia coli. Nucleic Acids Res 13:3213-3220.
    • (1985) Nucleic Acids Res , vol.13 , pp. 3213-3220
    • Kuchino, Y.1    Mori, F.2    Nishimura, S.3
  • 18
    • 0021759249 scopus 로고
    • Nucleotide sequences of three proline tRNAs from Salmonella typhimurium
    • Kuchino Y, Yabusaki Y, Mori F, Nishimura S. 1984. Nucleotide sequences of three proline tRNAs from Salmonella typhimurium. Nucleic Acids Res 12:1559-1562.
    • (1984) Nucleic Acids Res , vol.12 , pp. 1559-1562
    • Kuchino, Y.1    Yabusaki, Y.2    Mori, F.3    Nishimura, S.4
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0021921433 scopus 로고
    • Transformation of Salmonella typhimurium with plasmid DNA: Differences between rough and smooth strains
    • MacLachlan PR, Sanderson KE. 1985. Transformation of Salmonella typhimurium with plasmid DNA: Differences between rough and smooth strains. J Bacteriol 161:442-445.
    • (1985) J Bacteriol , vol.161 , pp. 442-445
    • MacLachlan, P.R.1    Sanderson, K.E.2
  • 22
    • 0030750024 scopus 로고    scopus 로고
    • Transfer RNA recognition by the Escherichia coli Delta(2)-isopentenyl-pyrophosphate: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)-isopentenyl-pyrophosphate: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
  • 23
    • 0028595685 scopus 로고
    • A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine 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 tRNA-guanine 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
  • 24
    • 0017357987 scopus 로고
    • Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli
    • Neidhardt FC, Bloch PL, Pedersen S, Reeh S. 1977. Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol 129:378-387.
    • (1977) J Bacteriol , vol.129 , pp. 378-387
    • Neidhardt, F.C.1    Bloch, P.L.2    Pedersen, S.3    Reeh, S.4
  • 26
    • 0014433108 scopus 로고
    • Nuclear magnetic resonance study of the interactions of guanosine and cytidine in dimethyl sulfoxide
    • Newmark RA, Cantor CR. 1968. Nuclear magnetic resonance study of the interactions of guanosine and cytidine in dimethyl sulfoxide. J Am Chem Soc 90:5010-5017.
    • (1968) J Am Chem Soc , vol.90 , pp. 5010-5017
    • Newmark, R.A.1    Cantor, C.R.2
  • 27
    • 0002157687 scopus 로고
    • Chromatographic mobilities of modified nucleosides
    • Schimmel PR, Söll D, Abelson JN, eds. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Nishimura S. 1979. Chromatographic mobilities of modified nucleosides. In: Schimmel PR, Söll D, Abelson JN, eds. Transfer RNA: Structure, properties, and recognition. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press. pp 551-552.
    • (1979) Transfer RNA: Structure, Properties, and Recognition , pp. 551-552
    • Nishimura, S.1
  • 28
    • 0031581873 scopus 로고    scopus 로고
    • GGG of Salmonella typhimurium
    • GGG 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
  • 30
    • 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
  • 31
    • 0014966535 scopus 로고
    • Suppressors of frameshift mutations in Salmonella typhimurium
    • Riddle DL, Roth JR. 1970. Suppressors of frameshift mutations in Salmonella typhimurium. J Mol Biol 54:131-144.
    • (1970) J Mol Biol , vol.54 , pp. 131-144
    • Riddle, D.L.1    Roth, J.R.2
  • 32
    • 0015527028 scopus 로고
    • Frameshift suppressors. III. Effects of suppressor mutations on transfer RNA
    • Riddle DL, Roth JR. 1972. Frameshift suppressors. III. Effects of suppressor mutations on transfer RNA. J Mol Biol 66:495-506.
    • (1972) J Mol Biol , vol.66 , pp. 495-506
    • Riddle, D.L.1    Roth, J.R.2
  • 33
    • 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
  • 34
    • 0015449701 scopus 로고
    • Phage P22-mutants with increased or decreased transduction abilities
    • Schmieger H. 1972. Phage P22-mutants with increased or decreased transduction abilities. Mol Gen Genet 119:75-88.
    • (1972) Mol Gen Genet , vol.119 , pp. 75-88
    • Schmieger, H.1
  • 37
    • 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
  • 38
    • 0026350896 scopus 로고
    • Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase
    • Varshney U, Lee CP, RajBhandary UL. 1991. Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase. J Biol Chem 266:24712-24718.
    • (1991) J Biol Chem , vol.266 , pp. 24712-24718
    • Varshney, U.1    Lee, C.P.2    Rajbhandary, U.L.3
  • 39
    • 0026528473 scopus 로고
    • Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae
    • von Pawel-Rammingen U, Åström S, Byström AS. 1992. Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae. Mol Cell Biol 12: 1432-1442.
    • (1992) Mol Cell Biol , vol.12 , pp. 1432-1442
    • Von Pawel-Rammingen, U.1    Åström, S.2    Byström, A.S.3
  • 40
    • 0023027061 scopus 로고
    • The translational efficiency of tRNA is a property of the anticodon arm
    • Yarus M, Cline S, Raftery L, Wier P, Bradley D. 1986. The translational efficiency of tRNA is a property of the anticodon arm. J Biol Chem 261:10496-10505.
    • (1986) J Biol Chem , vol.261 , pp. 10496-10505
    • Yarus, M.1    Cline, S.2    Raftery, L.3    Wier, P.4    Bradley, D.5


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