메뉴 건너뛰기




Volumn 32, Issue 13, 2004, Pages 4081-4089

Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; ARGININE; ASPARTYL TRANSFER RNA LIGASE; BETA GALACTOSIDASE; GLUTAMIC ACID; TRANSFER RNA; UNCLASSIFIED DRUG; AMINOACYL TRANSFER RNA; ASPARTATE TRANSFER RNA LIGASE; ASPARTIC ACID; TRNA, ASPARTIC ACID; TRNA, ASPARTIC ACID-;

EID: 3242890837     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh751     Document Type: Article
Times cited : (6)

References (56)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba,M. and Söll,D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 2
    • 0027444211 scopus 로고
    • Transfer RNA identity
    • McClain,W.H. (1993) Transfer RNA identity. FASEB J., 7, 72-78.
    • (1993) FASEB J. , vol.7 , pp. 72-78
    • McClain, W.H.1
  • 3
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giegé,R., Sissler,M. and Florentz,C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res., 26, 5017-5035. 4 Swanson,R., Hoben,P., Sumner-Smith,M., Uemura,H., Watson,L. and Söll,D. (1988) Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase. Science, 242, 1548-1551.
    • (1998) Nucleic Acids Res. , vol.242 , pp. 1548-1551
    • Giegé, R.1    Sissler, M.2    Florentz, C.3
  • 4
    • 0024239917 scopus 로고
    • Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase
    • Swanson,R., Hoben,P., Sumner-Smith,M., Uemura,H., Watson,L. and Söll,D. (1988) Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase. Science, 242, 1548-1551.
    • (1988) Science , vol.242 , pp. 1548-1551
    • Swanson, R.1    Hoben, P.2    Sumner-Smith, M.3    Uemura, H.4    Watson, L.5    Söll, D.6
  • 5
    • 0027074048 scopus 로고
    • Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants
    • Sherman,J.M., Rogers,K., Rogers,M.J. and Söll,D. (1992) Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. J. Mol. Biol., 228, 1055-1062.
    • (1992) J. Mol. Biol. , vol.228 , pp. 1055-1062
    • Sherman, J.M.1    Rogers, K.2    Rogers, M.J.3    Söll, D.4
  • 6
    • 0034618571 scopus 로고    scopus 로고
    • Domain-specific recruitment of amide amino acids for protein synthesis
    • Tumbula,D.L., Becker,H.D., Chang,W.Z. and Söll, D. (2000) Domain-specific recruitment of amide amino acids for protein synthesis. Nature, 407, 106-110.
    • (2000) Nature , vol.407 , pp. 106-110
    • Tumbula, D.L.1    Becker, H.D.2    Chang, W.Z.3    Söll, D.4
  • 8
    • 0022449958 scopus 로고
    • Glu in B. subtilis and efficiently misacylates E. coli tRNAGln in vitro
    • Glu in B. subtilis and efficiently misacylates E. coli tRNAGln in vitro. J. Bacteriol., 165, 88-93.
    • (1986) J. Bacteriol. , vol.165 , pp. 88-93
    • Lapointe, J.1    Duplain, L.2    Proulx, M.3
  • 9
    • 0032573150 scopus 로고    scopus 로고
    • T. thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways
    • Becker,H. and Kern,D. (1998) T. thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. Proc. Natl Acad. Sci. USA, 95, 12832-12837.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12832-12837
    • Becker, H.1    Kern, D.2
  • 10
    • 0035119935 scopus 로고    scopus 로고
    • Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase
    • Sekine,S., Nureki,O., Shimada,A., Vassylyev,D.G. and Yokoyama,S. (2001) Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Nature Struct. Biol., 8, 203-206.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 203-206
    • Sekine, S.1    Nureki, O.2    Shimada, A.3    Vassylyev, D.G.4    Yokoyama, S.5
  • 11
    • 0038286152 scopus 로고    scopus 로고
    • Expanding tRNA recognition of a tRNA synthetase by a single amino acid change
    • Feng,L., Tumbula-Hansen,D., Toogood,H. and Söll,D. (2003) Expanding tRNA recognition of a tRNA synthetase by a single amino acid change. Proc. Natl Acad. Sci. USA, 100, 5676-5681.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5676-5681
    • Feng, L.1    Tumbula-Hansen, D.2    Toogood, H.3    Söll, D.4
  • 13
  • 14
    • 0028908128 scopus 로고
    • Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide
    • Auld,D.S. and Schimmel,P. (1995) Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide. Science, 267, 1994-1996.
    • (1995) Science , vol.267 , pp. 1994-1996
    • Auld, D.S.1    Schimmel, P.2
  • 15
    • 0030005119 scopus 로고    scopus 로고
    • Single sequence of a helix-loop peptide confers functional anticodon recognition on two tRNA synthetases
    • Auld,D.S. and Schimmel,P. (1996) Single sequence of a helix-loop peptide confers functional anticodon recognition on two tRNA synthetases. EMBO J., 15, 1142-1148.
    • (1996) EMBO J. , vol.15 , pp. 1142-1148
    • Auld, D.S.1    Schimmel, P.2
  • 17
    • 0027488750 scopus 로고
    • Two acidic residues of Escherichia coli methionyl-tRNA synthetase act as negative discriminants towards the binding of non-cognate tRNA anticodons
    • Schmitt,E., Meinnel,T., Panvert,M., Mechulam,Y. and Blanquet,S. (1993) Two acidic residues of Escherichia coli methionyl-tRNA synthetase act as negative discriminants towards the binding of non-cognate tRNA anticodons. J. Mol. Biol., 233, 615-628.
    • (1993) J. Mol. Biol. , vol.233 , pp. 615-628
    • Schmitt, E.1    Meinnel, T.2    Panvert, M.3    Mechulam, Y.4    Blanquet, S.5
  • 18
    • 0042733155 scopus 로고    scopus 로고
    • Anticodon recognition in evolution: Switching tRNA specificity of an aminoacyl-tRNA synthetase by site-directed peptide transplantation
    • Brevet,A., Chen,J., Commans,S., Lazennec,C., Blanquet,S. and Plateau,P. (2003) Anticodon recognition in evolution: switching tRNA specificity of an aminoacyl-tRNA synthetase by site-directed peptide transplantation. J. Biol. Chem., 278, 30927-30935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30927-30935
    • Brevet, A.1    Chen, J.2    Commans, S.3    Lazennec, C.4    Blanquet, S.5    Plateau, P.6
  • 19
    • 0022310661 scopus 로고
    • The role of the anticodon in recognition of tRNA by aminoacyl-tRNA synthetases
    • Kisselev,L. (1985) The role of the anticodon in recognition of tRNA by aminoacyl-tRNA synthetases. Prog. Nucleic Acid Res. Mol. Biol., 32, 237-266.
    • (1985) Prog. Nucleic Acid Res. Mol. Biol. , vol.32 , pp. 237-266
    • Kisselev, L.1
  • 21
    • 0002607306 scopus 로고
    • XL1-red: A highly efficient random mutagenesis strain
    • Greener,A. and Callahan,M. (1994) XL1-red: a highly efficient random mutagenesis strain. Strateg. Mol. Biol. - Newslett., 7, 32-34.
    • (1994) Strateg. Mol. Biol. - Newslett. , vol.7 , pp. 32-34
    • Greener, A.1    Callahan, M.2
  • 22
    • 0020583709 scopus 로고
    • Effects of surrounding sequence on the suppression of nonsense codons
    • Miller,J.H. and Albertini,A.M. (1983) Effects of surrounding sequence on the suppression of nonsense codons. J. Mol. Biol., 164, 59-71.
    • (1983) J. Mol. Biol. , vol.164 , pp. 59-71
    • Miller, J.H.1    Albertini, A.M.2
  • 25
    • 0023787932 scopus 로고
    • pACYC184-derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids
    • Martinez,E., Bartolomé,B. and de la Cruz,F. (1988) pACYC184-derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids. Gene, 68, 159-162.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martinez, E.1    Bartolomé, B.2    de la Cruz, F.3
  • 26
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in E. coli
    • Aman,E., Ochs,B. and Abel,K.J. (1988) Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in E. coli. Gene, 69, 301-305.
    • (1988) Gene , vol.69 , pp. 301-305
    • Aman, E.1    Ochs, B.2    Abel, K.J.3
  • 29
    • 0025695388 scopus 로고
    • Aspartyl-tRNA synthetase from E. coli: Cloning and characterization of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases
    • Eriani,G., Dirheimer,G. and Gangloff,J. (1990) Aspartyl-tRNA synthetase from E. coli: cloning and characterization of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases. Nucleic Acids Res., 18, 7109-7117.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7109-7117
    • Eriani, G.1    Dirheimer, G.2    Gangloff, J.3
  • 30
    • 0024277927 scopus 로고
    • Anticodon switching changes the identity of methionine and valine transfer RNAs
    • Schulman,L.H. and 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
  • 32
    • 0033609807 scopus 로고    scopus 로고
    • Asp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs
    • Asp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs. J. Mol. Biol., 291, 761-773.
    • (1999) J. Mol. Biol. , vol.291 , pp. 761-773
    • Eriani, G.1    Gangloff, J.2
  • 34
    • 0033617251 scopus 로고    scopus 로고
    • Active site mapping of yeast aspartyl-tRNA synthetase by in vivo selection of enzyme mutations lethal for cell growth
    • Ador,L., Camasses,A., Erbs,P., Cavarelli,J., Moras,D., Gangloff,J. and Eriani,G. (1999) Active site mapping of yeast aspartyl-tRNA synthetase by in vivo selection of enzyme mutations lethal for cell growth. J. Mol. Biol., 288, 231-242.
    • (1999) J. Mol. Biol. , vol.288 , pp. 231-242
    • Ador, L.1    Camasses, A.2    Erbs, P.3    Cavarelli, J.4    Moras, D.5    Gangloff, J.6    Eriani, G.7
  • 35
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang,A.C.Y. and Cohen,S.N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol., 134, 1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 39
    • 0027769983 scopus 로고
    • Triple aminoacylation specificity of a chimerized transfer RNA
    • Frugier,M., Florentz,C., Schimmel,P. and Giegé,R. (1993) Triple aminoacylation specificity of a chimerized transfer RNA. Biochemistry, 32, 14053-14061.
    • (1993) Biochemistry , vol.32 , pp. 14053-14061
    • Frugier, M.1    Florentz, C.2    Schimmel, P.3    Giegé, R.4
  • 40
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin,A.G. (1993) OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 44
    • 0029907152 scopus 로고    scopus 로고
    • Lys transcript: Anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue
    • Lys transcript: anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue. EMBO J., 15, 6321-6334.
    • (1996) EMBO J. , vol.15 , pp. 6321-6334
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 45
    • 0033790766 scopus 로고    scopus 로고
    • A new orthogonal suppressor tRNA/aminoacyl-tRNA synthetase pair for evolving an organism with expanded genetic code
    • Pastrnak,M., Magliery,T.J. and Schultz,P.G. (2000) A new orthogonal suppressor tRNA/aminoacyl-tRNA synthetase pair for evolving an organism with expanded genetic code. Helv. Chim. Acta, 83, 2277-2286.
    • (2000) Helv. Chim. Acta , vol.83 , pp. 2277-2286
    • Pastrnak, M.1    Magliery, T.J.2    Schultz, P.G.3
  • 46
    • 2642524472 scopus 로고    scopus 로고
    • Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase
    • Ador,L., Jaeger,S., Geslain,R., Martin,F., Cavarelli,J. and Eriani,G. (2004) Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase. Biochemistry, 43, 7028-7037.
    • (2004) Biochemistry , vol.43 , pp. 7028-7037
    • Ador, L.1    Jaeger, S.2    Geslain, R.3    Martin, F.4    Cavarelli, J.5    Eriani, G.6
  • 47
    • 0015378783 scopus 로고
    • The frequency of errors in protein biosynthesis
    • Loftfield,R.B. and Vanderjagt,M.A. (1972) The frequency of errors in protein biosynthesis. Biochem. J., 128, 1353-1356.
    • (1972) Biochem. J , vol.128 , pp. 1353-1356
    • Loftfield, R.B.1    Vanderjagt, M.A.2
  • 48
    • 0017164328 scopus 로고
    • Theories of enzyme specificity and their application to proteases and aminoacyl-transfer RNA synthetases
    • Bosshard,H. (1992) Theories of enzyme specificity and their application to proteases and aminoacyl-transfer RNA synthetases. Experientia, 32, 949-963.
    • (1992) Experientia , vol.32 , pp. 949-963
    • Bosshard, H.1
  • 49
    • 0015885054 scopus 로고
    • Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA synthetase recognition and particular importance of the maximal velocity
    • Ebel,J.-P., Giegé,R., Bonnet,J., Kern,D., Befort,N., Bollack,C., Fasiolo,F., Gangloff,J. and Dirheimer,G. (1973) Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA synthetase recognition and particular importance of the maximal velocity. Biochimie, 55, 547-557.
    • (1973) Biochimie , vol.55 , pp. 547-557
    • Ebel, J.-P.1    Giegé, R.2    Bonnet, J.3    Kern, D.4    Befort, N.5    Bollack, C.6    Fasiolo, F.7    Gangloff, J.8    Dirheimer, G.9
  • 50
    • 0027976415 scopus 로고
    • Discrimination against misacylated tRNA by chloroplast elongation factor Tu
    • Stanzel,M., Schön,A. and Sprinzl,M. (1994) Discrimination against misacylated tRNA by chloroplast elongation factor Tu. Eur. J. Biochem., 219, 435-439.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 435-439
    • Stanzel, M.1    Schön, A.2    Sprinzl, M.3
  • 51
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • LaRiviere,F.J., Wolfson,A.D. and Uhlenbeck,O.C. (2001) Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science, 294, 165-168.
    • (2001) Science , vol.294 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 52
    • 0027992228 scopus 로고
    • Evolution of the Glx-tRNA synthetase family: The glutaminyl enzyme as a case of horizontal gene transfer
    • Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and Mirande,M. (1994) Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc. Natl Acad. Sci. USA, 91, 8670-8674.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8670-8674
    • Lamour, V.1    Quevillon, S.2    Diriong, S.3    N'Guyen, V.C.4    Lipinski, M.5    Mirande, M.6
  • 53
    • 0033607138 scopus 로고    scopus 로고
    • Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains
    • Chihade,J.W. and Schimmel,P. (1999) Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains. Proc. Natl Acad. Sci. USA, 96, 12316-12321.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12316-12321
    • Chihade, J.W.1    Schimmel, P.2
  • 54
    • 0038272086 scopus 로고    scopus 로고
    • RNA recognition by designed peptide fusion creates 'artificial' tRNA synthetase
    • Frugier,M., Giegé,R. and Schimmel,P. (2003) RNA recognition by designed peptide fusion creates 'artificial' tRNA synthetase. Proc. Natl Acad. Sci. USA, 100, 7471-7475.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7471-7475
    • Frugier, M.1    Giegé, R.2    Schimmel, P.3
  • 56
    • 0032830481 scopus 로고    scopus 로고
    • Evolution of aminoacyl-tRNA synthetases-analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events
    • Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V. (1999) Evolution of aminoacyl-tRNA synthetases-analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res., 9, 689-710.
    • (1999) Genome Res. , vol.9 , pp. 689-710
    • Wolf, Y.I.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.