메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 95-101

The many routes of bacterial transfer RNAs after aminoacylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL RNA; TRANSFER RNA;

EID: 0033962666     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00055-X     Document Type: Review
Times cited : (14)

References (51)
  • 1
    • 0031456444 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases
    • Cusack S. Aminoacyl-tRNA synthetases. Curr Opin Struct Biol. 7:1997;881-889.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 881-889
    • Cusack, S.1
  • 2
    • 0014219470 scopus 로고
    • D-tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis
    • Calendar R., Berg P. D-tyrosyl RNA: formation, hydrolysis and utilization for protein synthesis. J Mol Biol. 26:1967;39-54.
    • (1967) J Mol Biol , vol.26 , pp. 39-54
    • Calendar, R.1    Berg, P.2
  • 5
    • 0018780572 scopus 로고
    • Establishing the misaminoacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases
    • Fersht A.R., Dingwall C. Establishing the misaminoacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases. Biochemistry. 18:1979;1238-1245.
    • (1979) Biochemistry , vol.18 , pp. 1238-1245
    • Fersht, A.R.1    Dingwall, C.2
  • 6
    • 0003481596 scopus 로고
    • A.R. Fersht. San Francisco: WH Freeman and Co
    • Fersht A.R. Enzyme Structure and Mechanism. 1977;282-283 WH Freeman and Co, San Francisco.
    • (1977) Enzyme Structure and Mechanism , pp. 282-283
  • 8
    • 0032562707 scopus 로고    scopus 로고
    • Sieves in sequence
    • Fersht A.R. Sieves in sequence. Science. 280:1998;541.
    • (1998) Science , vol.280 , pp. 541
    • Fersht, A.R.1
  • 9
    • 0029854940 scopus 로고    scopus 로고
    • Aminoacylation error correction
    • Lin L., Hale S.P., Schimmel P. Aminoacylation error correction. Nature. 384:1996;33-34.
    • (1996) Nature , vol.384 , pp. 33-34
    • Lin, L.1    Hale, S.P.2    Schimmel, P.3
  • 10
    • 0033551859 scopus 로고    scopus 로고
    • Ile and mupirocin
    • The authors reveal the structure of isoleucine-tRNA synthetase complexed with tRNA. The structure suggests a dynamical mechanism for the correction of aminoacylation errors
    • Ile and mupirocin. Science. 285:1999;1074-1077. The authors reveal the structure of isoleucine-tRNA synthetase complexed with tRNA. The structure suggests a dynamical mechanism for the correction of aminoacylation errors.
    • (1999) Science , vol.285 , pp. 1074-1077
    • Silvian, L.F.1    Wang, J.2    Steitz, T.A.3
  • 11
  • 12
    • 0001314696 scopus 로고
    • The selenocysteine-inserting tRNA species: Structure and function
    • D. Söll, & U.L. RajBhandary. Washington, DC: American Society for Microbiology
    • Baron C., Böck A. The selenocysteine-inserting tRNA species: structure and function. Söll D., RajBhandary U.L. tRNA: Structure, Biosynthesis, and Function. 1995;529-544 American Society for Microbiology, Washington, DC.
    • (1995) TRNA: Structure, Biosynthesis, and Function , pp. 529-544
    • Baron, C.1    Böck, A.2
  • 13
    • 0001239924 scopus 로고
    • Opal suppressor serine tRNAs from bovine liver form phosphoseryl-tRNA
    • Hatfield D., Diamond A., Dudock B. Opal suppressor serine tRNAs from bovine liver form phosphoseryl-tRNA. Proc Natl Acad Sci USA. 79:1982;6215-6219.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6215-6219
    • Hatfield, D.1    Diamond, A.2    Dudock, B.3
  • 14
    • 0030592461 scopus 로고    scopus 로고
    • Selenocysteine synthesis in mammalia: An identity switch from tRNA(Ser) to tRNA(Sec)
    • Amberg R., Mizutani T., Wu X.Q., Gross H.J. Selenocysteine synthesis in mammalia: an identity switch from tRNA(Ser) to tRNA(Sec). J Mol Biol. 263:1996;8-19.
    • (1996) J Mol Biol , vol.263 , pp. 8-19
    • Amberg, R.1    Mizutani, T.2    Wu, X.Q.3    Gross, H.J.4
  • 15
    • 0032724547 scopus 로고    scopus 로고
    • A SECIS binding protein (SBP) is distinct from selenocysteyl-tRNA protecting factor (SePF)
    • Fujiwara T., Busch K., Gross H.J., Mizutani T. A SECIS binding protein (SBP) is distinct from selenocysteyl-tRNA protecting factor (SePF). Biochimie. 81:1999;213-218.
    • (1999) Biochimie , vol.81 , pp. 213-218
    • Fujiwara, T.1    Busch, K.2    Gross, H.J.3    Mizutani, T.4
  • 17
    • 0025736565 scopus 로고
    • Selenocysteine synthase from Escherichia coli: Analysis of the reaction sequence
    • Forchhammer K., Böck A. Selenocysteine synthase from Escherichia coli: analysis of the reaction sequence. J Biol Chem. 266:1991;6324-6328.
    • (1991) J Biol Chem , vol.266 , pp. 6324-6328
    • Forchhammer, K.1    Böck, A.2
  • 18
    • 0032211950 scopus 로고    scopus 로고
    • The dual identities of mammalian tRNASec for SerRS and selenocysteine synthase
    • Mizutani T., Kanaya K., Ikeda S., Fujiwara T., Yamada K., Totsuka T. The dual identities of mammalian tRNASec for SerRS and selenocysteine synthase. Mol Biol Rep. 25:1998;211-216.
    • (1998) Mol Biol Rep , vol.25 , pp. 211-216
    • Mizutani, T.1    Kanaya, K.2    Ikeda, S.3    Fujiwara, T.4    Yamada, K.5    Totsuka, T.6
  • 19
    • 0027298176 scopus 로고
    • Unique secondary and tertiary structural features of the eucaryotic selenocysteine tRNA(Sec)
    • Sturchler C., Westhof E., Carbon P., Krol A. Unique secondary and tertiary structural features of the eucaryotic selenocysteine tRNA(Sec). Nucleic Acids Res. 21:1993;1073-1079.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1073-1079
    • Sturchler, C.1    Westhof, E.2    Carbon, P.3    Krol, A.4
  • 21
    • 0029781454 scopus 로고    scopus 로고
    • TRNA-dependent asparagine formation
    • Curnow A.W., Ibba M., Söll D. tRNA-dependent asparagine formation. Nature. 382:1996;589-590.
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Söll, D.3
  • 22
    • 0024285823 scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • Schön A., Kannangara C.G., Gough S., Söll D. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature. 331:1988;187-190.
    • (1988) Nature , vol.331 , pp. 187-190
    • Schön, A.1    Kannangara, C.G.2    Gough, S.3    Söll, D.4
  • 23
    • 0032573080 scopus 로고    scopus 로고
    • Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
    • Curnow A.W., Tumbula D.L., Pelaschier J.T., Min B., Söll D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proc Natl Acad Sci USA. 95:1998;12838-12843.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12838-12843
    • Curnow, A.W.1    Tumbula, D.L.2    Pelaschier, J.T.3    Min, B.4    Söll, D.5
  • 25
    • 0031984643 scopus 로고    scopus 로고
    • Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase
    • Nakatsu T., Kato H., Oda J. Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase. Nat Struct Biol. 5:1998;15-19.
    • (1998) Nat Struct Biol , vol.5 , pp. 15-19
    • Nakatsu, T.1    Kato, H.2    Oda, J.3
  • 26
    • 0029816343 scopus 로고    scopus 로고
    • Met formyltransferase: Comparison with glycinamide ribonucleotide formyltransferase
    • Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase. EMBO J. 15:1996;4749-4758.
    • (1996) EMBO J , vol.15 , pp. 4749-4758
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 28
    • 0031471225 scopus 로고    scopus 로고
    • Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase: Role of a 16-amino acid insertion module in initiator tRNA recognition
    • Ramesh V., Gite S., Li Y., RajBhandary U.L. Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase: role of a 16-amino acid insertion module in initiator tRNA recognition. Proc Natl Acad Sci USA. 94:1997;13524-13529.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13524-13529
    • Ramesh, V.1    Gite, S.2    Li, Y.3    Rajbhandary, U.L.4
  • 29
    • 0032506057 scopus 로고    scopus 로고
    • Functional interaction of an arginine conserved in the sixteen amino acid insertion module of Escherichia coli methionyl-tRNA formyltransferase with determinants for formylation in the initiator tRNA
    • Ramesh V., Gite S., RajBhandary U.L. Functional interaction of an arginine conserved in the sixteen amino acid insertion module of Escherichia coli methionyl-tRNA formyltransferase with determinants for formylation in the initiator tRNA. Biochemistry. 37:1998;15925-15932.
    • (1998) Biochemistry , vol.37 , pp. 15925-15932
    • Ramesh, V.1    Gite, S.2    Rajbhandary, U.L.3
  • 31
    • 0029787494 scopus 로고    scopus 로고
    • Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli
    • Guillon J.M., Heiss S., Suturina J., Mechulam Y., Laalami S., Grunberg-Manago M., Blanquet S. Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli. J Biol Chem. 271:1996;22321-22325.
    • (1996) J Biol Chem , vol.271 , pp. 22321-22325
    • Guillon, J.M.1    Heiss, S.2    Suturina, J.3    Mechulam, Y.4    Laalami, S.5    Grunberg-Manago, M.6    Blanquet, S.7
  • 33
    • 0033081413 scopus 로고    scopus 로고
    • The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
    • A comparison of the structures of two ternary complexes of EF-Tu·GDPNP indicates that subtle adaptations of EF-Tu can optimise the binding of any elongator tRNA
    • Nissen P., Thirup S., Kjeldgaard M., Nyborg J. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure. 7:1999;143-156. A comparison of the structures of two ternary complexes of EF-Tu·GDPNP indicates that subtle adaptations of EF-Tu can optimise the binding of any elongator tRNA.
    • (1999) Structure , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 34
    • 0029671252 scopus 로고    scopus 로고
    • Antideterminants present in minihelix(Sec) hinder its recognition by prokaryotic elongation factor Tu
    • Rudinger J., Hillenbrandt R., Sprinzl M., Giege R. Antideterminants present in minihelix(Sec) hinder its recognition by prokaryotic elongation factor Tu. EMBO J. 15:1996;650-657.
    • (1996) EMBO J , vol.15 , pp. 650-657
    • Rudinger, J.1    Hillenbrandt, R.2    Sprinzl, M.3    Giege, R.4
  • 35
    • 0028034499 scopus 로고
    • Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination
    • Astrom S.U., Bystrom A.S. Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination. Cell. 79:1994;535-546.
    • (1994) Cell , vol.79 , pp. 535-546
    • Astrom, S.U.1    Bystrom, A.S.2
  • 36
    • 0031952186 scopus 로고    scopus 로고
    • Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis
    • Drabkin H.J., Estrella M., Rajbhandary U.L. Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis. Mol Cell Biol. 18:1998;1459-1466.
    • (1998) Mol Cell Biol , vol.18 , pp. 1459-1466
    • Drabkin, H.J.1    Estrella, M.2    Rajbhandary, U.L.3
  • 37
    • 0027976415 scopus 로고
    • Discrimination against misacylated tRNA by chloroplast elongation factor Tu
    • Stanzel M., Schon A., Sprinzl M. Discrimination against misacylated tRNA by chloroplast elongation factor Tu. Eur J Biochem. 219:1994;435-439.
    • (1994) Eur J Biochem , vol.219 , pp. 435-439
    • Stanzel, M.1    Schon, A.2    Sprinzl, M.3
  • 38
    • 0032573150 scopus 로고    scopus 로고
    • Thermus thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways
    • Becker H.D., Kern D. Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. Proc Natl Acad Sci USA. 95:1998;12832-12837.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12832-12837
    • Becker, H.D.1    Kern, D.2
  • 39
    • 0030738859 scopus 로고    scopus 로고
    • Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase
    • Schmitt E., Mechulam Y., Fromant M., Plateau P., Blanquet S. Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. EMBO J. 16:1997;4760-4769.
    • (1997) EMBO J , vol.16 , pp. 4760-4769
    • Schmitt, E.1    Mechulam, Y.2    Fromant, M.3    Plateau, P.4    Blanquet, S.5
  • 40
    • 0027169358 scopus 로고
    • Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase
    • Dutka S., Meinnel T., Lazennec C., Mechulam Y., Blanquet S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucleic Acids Res. 21:1993;4025-4030.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4025-4030
    • Dutka, S.1    Meinnel, T.2    Lazennec, C.3    Mechulam, Y.4    Blanquet, S.5
  • 41
    • 0016612582 scopus 로고
    • The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase
    • Schulman L.H., Pelka H. The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase. J Biol Chem. 250:1975;542-547.
    • (1975) J Biol Chem , vol.250 , pp. 542-547
    • Schulman, L.H.1    Pelka, H.2
  • 42
    • 0033586788 scopus 로고    scopus 로고
    • Receptor site for the 5′-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolase
    • This study, together with [41], provides the basis for the proposal that a 5′ phosphate on the top of a full 1-72 base pair in elongator tRNAs plays the role of an identity determinant in the generic recognition of elongator tRNAs by translational protein factors
    • Fromant M., Plateau P., Schmitt E., Mechulam Y., Blanquet S. Receptor site for the 5′-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolase. Biochemistry. 38:1999;4982-4987. This study, together with [41], provides the basis for the proposal that a 5′ phosphate on the top of a full 1-72 base pair in elongator tRNAs plays the role of an identity determinant in the generic recognition of elongator tRNAs by translational protein factors.
    • (1999) Biochemistry , vol.38 , pp. 4982-4987
    • Fromant, M.1    Plateau, P.2    Schmitt, E.3    Mechulam, Y.4    Blanquet, S.5
  • 43
    • 0025954795 scopus 로고
    • Molecular dissection of translation initiation factor IF2. Evidence for two structural and functional domains
    • Gualerzi C.O., Severini M., Spurio R., La Teana A., Pon C.L. Molecular dissection of translation initiation factor IF2. Evidence for two structural and functional domains. J Biol Chem. 266:1991;16356-16362.
    • (1991) J Biol Chem , vol.266 , pp. 16356-16362
    • Gualerzi, C.O.1    Severini, M.2    Spurio, R.3    La Teana, A.4    Pon, C.L.5
  • 44
    • 0033525871 scopus 로고    scopus 로고
    • In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling
    • Luchin S., Putzer H., Hershey J.W., Cenatiempo Y., Grunberg-Manago M., Laalami S. In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling. J Biol Chem. 274:1999;6074-6079.
    • (1999) J Biol Chem , vol.274 , pp. 6074-6079
    • Luchin, S.1    Putzer, H.2    Hershey, J.W.3    Cenatiempo, Y.4    Grunberg-Manago, M.5    Laalami, S.6
  • 45
    • 0343754659 scopus 로고    scopus 로고
    • Preliminary characterisation by X-ray diffraction and Raman spectroscopy of a crystalline complex of Bacillus stearothermophilus initiation factor 2 C-domain and fMet-tRNAfMet
    • Forster C., Krafft C., Welfle H., Gualerzi C.O., Heinemann U. Preliminary characterisation by X-ray diffraction and Raman spectroscopy of a crystalline complex of Bacillus stearothermophilus initiation factor 2 C-domain and fMet-tRNAfMet. Acta Crystallogr. D55:1999;712-716.
    • (1999) Acta Crystallogr , vol.55 , pp. 712-716
    • Forster, C.1    Krafft, C.2    Welfle, H.3    Gualerzi, C.O.4    Heinemann, U.5
  • 46
    • 0031854151 scopus 로고    scopus 로고
    • Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors
    • Brock S., Szkaradkiewicz K., Sprinzl M. Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors. Mol Microbiol. 29:1998;409-417.
    • (1998) Mol Microbiol , vol.29 , pp. 409-417
    • Brock, S.1    Szkaradkiewicz, K.2    Sprinzl, M.3
  • 50
    • 13044292050 scopus 로고    scopus 로고
    • Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2
    • This communication introduces the idea that a eubacterial-type IF2 is universally involved in the presentation of initiator tRNA to the ribosomal P site
    • Lee J.H., Choi S.K., Roll-Mecak A., Burley S.K., Dever T.E. Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2. Proc Natl Acad Sci USA. 96:1999;4342-4347. This communication introduces the idea that a eubacterial-type IF2 is universally involved in the presentation of initiator tRNA to the ribosomal P site.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4342-4347
    • Lee, J.H.1    Choi, S.K.2    Roll-Mecak, A.3    Burley, S.K.4    Dever, T.E.5
  • 51
    • 0027609916 scopus 로고
    • Setor: Hardware lighted three-dimensional solid model representation of macromolecules
    • Evans S.V. Setor: hardware lighted three-dimensional solid model representation of macromolecules. J Mol Graphics. 11:1993;134-138.
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.