메뉴 건너뛰기




Volumn 41, Issue 2, 2013, Pages 1104-1112

Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; PHENYLALANINE TRANSFER RNA LIGASE; TRANSFER RNA;

EID: 84875460684     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1240     Document Type: Article
Times cited : (36)

References (46)
  • 1
    • 42049086762 scopus 로고    scopus 로고
    • Rate and accuracy of bacterial protein synthesis revisited
    • Johansson, M., Lovmar, M. and Ehrenberg, M. (2008) Rate and accuracy of bacterial protein synthesis revisited. Curr. Opin. Microbiol., 11, 141-147.
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 141-147
    • Johansson, M.1    Lovmar, M.2    Ehrenberg, M.3
  • 2
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • DOI 10.1074/jbc.R400006200
    • Kunkel, T.A. (2004) DNA replication fidelity. J. Biol. Chem., 279, 16895-16898. (Pubitemid 38560439)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 16895-16898
    • Kunkel, T.A.1
  • 3
    • 0022973817 scopus 로고
    • An RNA polymerase mutant with reduced accuracy of chain elongation
    • DOI 10.1021/bi00368a013
    • Blank, A., Gallant, J.A., Burgess, R.R. and Loeb, L.A. (1986) An RNA polymerase mutant with reduced accuracy of chain elongation. Biochemistry, 25, 5920-5928. (Pubitemid 17204024)
    • (1986) Biochemistry , vol.25 , Issue.20 , pp. 5920-5928
    • Blank, A.1    Gallant, J.A.2    Burgess, R.R.3    Loeb, L.A.4
  • 4
    • 0015378783 scopus 로고
    • The frequency of errors in protein biosynthesis
    • Loftfield, R.B. and Vanderjagt, D. (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, D.2
  • 5
    • 33845895536 scopus 로고    scopus 로고
    • The frequency of translational misreading errors in E. coli is largely determined by tRNA competition
    • DOI 10.1261/rna.294907
    • Kramer, E.B. and Farabaugh, P.J. (2007) The frequency of translational misreading errors in E. coli is largely determined by tRNA competition. RNA, 13, 87-96. (Pubitemid 46026183)
    • (2007) RNA , vol.13 , Issue.1 , pp. 87-96
    • Kramer, E.B.1    Farabaugh, P.J.2
  • 6
    • 70349545940 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis and translational quality control
    • Ling, J., Reynolds, N. and Ibba, M. (2009) Aminoacyl-tRNA synthesis and translational quality control. Annu. Rev. Microbiol., 63, 61-78.
    • (2009) Annu. Rev. Microbiol , vol.63 , pp. 61-78
    • Ling, J.1    Reynolds, N.2    Ibba, M.3
  • 7
    • 79955113244 scopus 로고    scopus 로고
    • Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding
    • Schrader, J.M., Chapman, S.J. and Uhlenbeck, O.C. (2011) Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding. Proc. Natl Acad. Sci. USA, 108, 5215-5220.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5215-5220
    • Schrader, J.M.1    Chapman, S.J.2    Uhlenbeck, O.C.3
  • 8
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: Lessons from protein synthesis
    • Zaher, H.S. and Green, R. (2009) Fidelity at the molecular level: lessons from protein synthesis. Cell, 136, 746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 9
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M. and Sö ll, 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
  • 11
    • 84855892823 scopus 로고    scopus 로고
    • Quality control in aminoacyl-tRNA synthesis its role in translational fidelity
    • Yadavalli, S.S. and Ibba, M. (2012) Quality control in aminoacyl-tRNA synthesis its role in translational fidelity. Adv. Protein Chem. Struct. Biol., 86, 1-43.
    • (2012) Adv. Protein Chem. Struct. Biol , vol.86 , pp. 1-43
    • Yadavalli, S.S.1    Ibba, M.2
  • 12
    • 2342431929 scopus 로고    scopus 로고
    • Lapointe, J. and Brakier-Gingras, L. (eds) Kluwer Academic/Plenum Publishers, New York, NY
    • Hendrickson, T.L. and Schimmel, P. (2003) In: Lapointe, J. and Brakier-Gingras, L. (eds), Translation Mechanisms. Kluwer Academic/Plenum Publishers, New York, NY, pp. 34-64.
    • (2003) Translation Mechanisms , pp. 34-64
    • Hendrickson, T.L.1    Schimmel, P.2
  • 14
    • 0017326738 scopus 로고
    • Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl tRNA synthetase
    • Fersht, A.R. (1977) Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry, 16, 1025-1030. (Pubitemid 8054893)
    • (1977) Biochemistry , vol.16 , Issue.5 , pp. 1025-1030
    • Fersht, A.R.1
  • 15
    • 0018788756 scopus 로고
    • Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases
    • Fersht, A.R. and Dingwall, C. (1979) Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases. Biochemistry, 18, 2627-2631.
    • (1979) Biochemistry , vol.18 , pp. 2627-2631
    • Fersht, A.R.1    Dingwall, C.2
  • 16
  • 17
    • 10644277147 scopus 로고    scopus 로고
    • Post-transfer editing in vitro and in vivo by the β subunit of phenylalanyl-tRNA synthetase
    • DOI 10.1038/sj.emboj.7600474
    • Roy, H., Ling, J., Irnov, M. and Ibba, M. (2004) Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J., 23, 4639-4648. (Pubitemid 39657863)
    • (2004) EMBO Journal , vol.23 , Issue.23 , pp. 4639-4648
    • Roy, H.1    Ling, J.2    Irnov, M.3    Ibba, M.4
  • 20
    • 33749669848 scopus 로고    scopus 로고
    • Global Effects of Mistranslation from an Editing Defect in Mammalian Cells
    • DOI 10.1016/j.chembiol.2006.08.011, PII S107455210600305X
    • Nangle, L.A., Motta, C.M. and Schimmel, P. (2006) Global effects of mistranslation from an editing defect in mammalian cells. Chem. Biol., 13, 1091-1100. (Pubitemid 44557071)
    • (2006) Chemistry and Biology , vol.13 , Issue.10 , pp. 1091-1100
    • Nangle, L.A.1    Motta, C.M.2    Schimmel, P.3
  • 23
    • 33645126396 scopus 로고    scopus 로고
    • Evolution of the genetic code in yeasts
    • Miranda, I., Silva, R. and Santos, M.A. (2006) Evolution of the genetic code in yeasts. Yeast, 23, 203-213.
    • (2006) Yeast , vol.23 , pp. 203-213
    • Miranda, I.1    Silva, R.2    Santos, M.A.3
  • 24
    • 79955558384 scopus 로고    scopus 로고
    • Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase
    • Jones, T.E., Alexander, R.W. and Pan, T. (2011) Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase. Proc. Natl Acad. Sci. USA, 108, 6933-6938.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 6933-6938
    • Jones, T.E.1    Alexander, R.W.2    Pan, T.3
  • 26
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling, J. and Sö ll, D. (2010) Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc. Natl Acad. Sci. USA, 107, 4028-4033.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4028-4033
    • Ling, J.1    Söll, D.2
  • 28
    • 79959348607 scopus 로고    scopus 로고
    • Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites
    • Li, L., Boniecki, M.T., Jaffe, J.D., Imai, B.S., Yau, P.M., Luthey-Schulten, Z.A. and Martinis, S.A. (2011) Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites. Proc. Natl Acad. Sci. USA, 108, 9378-9383.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9378-9383
    • Li, L.1    Boniecki, M.T.2    Jaffe, J.D.3    Imai, B.S.4    Yau, P.M.5    Luthey-Schulten, Z.A.6    Martinis, S.A.7
  • 29
    • 33644677385 scopus 로고    scopus 로고
    • Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase
    • DOI 10.1074/jbc.M508281200
    • Roy, H., Ling, J., Alfonzo, J. and Ibba, M. (2005) Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. J. Biol. Chem., 280, 38186-38192. (Pubitemid 43853713)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38186-38192
    • Roy, H.1    Ling, J.2    Alfonzo, J.3    Ibba, M.4
  • 30
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson, J.R. and Uhlenbeck, O.C. (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
  • 31
    • 33746189733 scopus 로고    scopus 로고
    • Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases
    • DOI 10.1016/j.jmb.2006.06.015, PII S002228360600725X
    • Zhang, C.M., Perona, J.J., Ryu, K., Francklyn, C. and Hou, Y.M. (2006) Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases. J. Mol. Biol., 361, 300-311. (Pubitemid 44092779)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.2 , pp. 300-311
    • Zhang, C.-M.1    Perona, J.J.2    Ryu, K.3    Francklyn, C.4    Hou, Y.-M.5
  • 32
    • 0026824909 scopus 로고
    • Identification of the pheS 5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37
    • Kast, P., Keller, B. and Hennecke, H. (1992) Identification of the pheS 5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37. J. Bacteriol., 174, 1686-1689.
    • (1992) J. Bacteriol , vol.174 , pp. 1686-1689
    • Kast, P.1    Keller, B.2    Hennecke, H.3
  • 34
    • 28844461982 scopus 로고    scopus 로고
    • Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase
    • DOI 10.1016/j.str.2005.08.013, PII S0969212605003564
    • Kotik-Kogan, O., Moor, N., Tworowski, D. and Safro, M. (2005) Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase. Structure, 13, 1799-1807. (Pubitemid 41772948)
    • (2005) Structure , vol.13 , Issue.12 , pp. 1799-1807
    • Kotik-Kogan, O.1    Moor, N.2    Tworowski, D.3    Safro, M.4
  • 35
    • 33746603054 scopus 로고    scopus 로고
    • Phenylalanyl-tRNA synthetase contains a dispensable RNA-binding domain that contributes to the editing of noncognate aminoacyl-tRNA
    • DOI 10.1021/bi060549w
    • Roy, H. and Ibba, M. (2006) Phenylalanyl-tRNA synthetase contains a dispensable RNA binding domain that contributes to editing of non-cognate aminoacyl-tRNA. Biochemistry, 45, 9156-9162. (Pubitemid 44156378)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9156-9162
    • Roy, H.1    Ibba, M.2
  • 36
    • 0019958076 scopus 로고
    • Catalytic mechanism of phenylalanyl-tRNA synthetase of Escherichia coli K10. Conformational change and tRNA(Phe) phenylalanylation are concerted
    • DOI 10.1021/bi00539a028
    • Baltzinger, M. and Holler, E. (1982) Catalytic mechanism of phenylalanyl-tRNA synthetase of Escherichia coli K10. Conformational change and tRNAPhe phenylalanylation are concerted. Biochemistry, 21, 2467-2476. (Pubitemid 12065048)
    • (1982) Biochemistry , vol.21 , Issue.10 , pp. 2467-2476
    • Baltzinger, M.1    Holler, E.2
  • 37
    • 0019965744 scopus 로고
    • Kinetics of acyl transfer ribonucleic acid complexes of Escherichia coli phenylalanyl-tRNA synthetase. A conformational change is rate limiting in catalysis
    • DOI 10.1021/bi00539a027
    • Baltzinger, M. and Holler, E. (1982) Kinetics of acyl transfer ribonucleic acid complexes of Escherichia coli phenylalanyl-tRNA synthetase. A conformational change is rate limiting in catalysis. Biochemistry, 21, 2460-2467. (Pubitemid 12065047)
    • (1982) Biochemistry , vol.21 , Issue.10 , pp. 2460-2467
    • Baltzinger, M.1    Holler, E.2
  • 38
    • 0028926480 scopus 로고
    • Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase
    • Ibba, M., Johnson, C.M., Hennecke, H. and Fersht, A.R. (1995) Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase. FEBS Lett., 358, 293-296.
    • (1995) FEBS Lett , vol.358 , pp. 293-296
    • Ibba, M.1    Johnson, C.M.2    Hennecke, H.3    Fersht, A.R.4
  • 39
    • 84859505162 scopus 로고    scopus 로고
    • Coordination of tRNA synthetase active sites for chemical fidelity
    • Boniecki, M.T. and Martinis, S.A. (2012) Coordination of tRNA synthetase active sites for chemical fidelity. J. Biol. Chem., 287, 11285-11289.
    • (2012) J. Biol. Chem , vol.287 , pp. 11285-11289
    • Boniecki, M.T.1    Martinis, S.A.2
  • 40
    • 84864341793 scopus 로고    scopus 로고
    • Speed, dissipation, and error in kinetic proofreading
    • Murugan, A., Huse, D.A. and Leibler, S. (2012) Speed, dissipation, and error in kinetic proofreading. Proc. Natl Acad. Sci. USA, 109, 12034-12039.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 12034-12039
    • Murugan, A.1    Huse, D.A.2    Leibler, S.3
  • 41
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield, J.J. (1974) Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl Acad. Sci. USA, 71, 4135-4139.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 42
    • 0029796028 scopus 로고    scopus 로고
    • Molecular biology of mycoplasmas
    • DOI 10.1146/annurev.micro.50.1.25
    • Dybvig, K. and Voelker, L.L. (1996) Molecular biology of mycoplasmas. Annu. Rev. Microbiol., 50, 25-57. (Pubitemid 26337458)
    • (1996) Annual Review of Microbiology , vol.50 , pp. 25-57
    • Dybvig, K.1    Voelker, L.L.2
  • 43
    • 0031593216 scopus 로고    scopus 로고
    • Influence of genomic G + C content on average amino-acid composition of proteins from 59 bacterial species
    • DOI 10.1016/S0378-1119(97)00403-4, PII S0378111997004034
    • Lobry, J.R. (1997) Influence of genomic G+C content on average amino-acid composition of proteins from 59 bacterial species. Gene, 205, 309-316. (Pubitemid 28029625)
    • (1997) Gene , vol.205 , Issue.1-2 , pp. 309-316
    • Lobry, J.R.1
  • 44
    • 0033745103 scopus 로고    scopus 로고
    • Nucleotide bias causes a genomewide bias in the amino acid composition of proteins
    • Singer, G.A. and Hickey, D.A. (2000) Nucleotide bias causes a genomewide bias in the amino acid composition of proteins. Mol. Biol. Evol., 17, 1581-1588.
    • (2000) Mol. Biol. Evol , vol.17 , pp. 1581-1588
    • Singer, G.A.1    Hickey, D.A.2
  • 45
    • 77954298382 scopus 로고    scopus 로고
    • Hyperaccurate and error-prone ribosomes exploit distinct mechanisms during tRNA selection
    • Zaher, H.S. and Green, R. (2010) Hyperaccurate and error-prone ribosomes exploit distinct mechanisms during tRNA selection. Mol. Cell, 39, 110-120.
    • (2010) Mol. Cell , vol.39 , pp. 110-120
    • Zaher, H.S.1    Green, R.2
  • 46
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: support, controversy, refinement and extension
    • DOI 10.1016/j.it.2006.06.008, PII S1471490606001785
    • Yewdell, J.W. and Nicchitta, C.V. (2006) The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol., 27, 368-373. (Pubitemid 44038666)
    • (2006) Trends in Immunology , vol.27 , Issue.8 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.