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Volumn 289, Issue 25, 2014, Pages 17780-17790

Reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; MAMMALS; QUALITY CONTROL;

EID: 84903449324     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.564609     Document Type: Article
Times cited : (20)

References (39)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M., and Soll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69, 617-650
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 4
    • 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
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giegé, R.1    Sissler, M.2    Florentz, C.3
  • 5
    • 33847023388 scopus 로고    scopus 로고
    • Kinetic Discrimination of tRNA Identity by the Conserved Motif 2 Loop of a Class II Aminoacyl-tRNA Synthetase
    • DOI 10.1016/j.molcel.2007.01.015, PII S1097276507000378
    • Guth, E. C., and Francklyn, C. S. (2007) Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Mol. Cell 25, 531-542 (Pubitemid 46274444)
    • (2007) Molecular Cell , vol.25 , Issue.4 , pp. 531-542
    • Guth, E.C.1    Francklyn, C.S.2
  • 6
    • 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
  • 7
    • 0021828928 scopus 로고
    • Hydrogen bonding and biological specificity analysed by protein engineering
    • DOI 10.1038/314235a0
    • Fersht, A. R., Shi, J. P., Knill-Jones, J., Lowe, D. M., Wilkinson, A. J., Blow, D. M., Brick, P., Carter, P., Waye, M. M., and Winter, G. (1985) Hydrogen bonding and biological specificity analysed by protein engineering. Nature 314, 235-238 (Pubitemid 15076511)
    • (1985) Nature , vol.314 , Issue.6008 , pp. 235-238
    • Fersht, A.R.1    Shi, J.P.2    Knill-Jones, J.3
  • 8
    • 0027104840 scopus 로고
    • Translational accuracy and the fitness of bacteria
    • Kurland, C. G. (1992) Translational accuracy and the fitness of bacteria. Annu. Rev. Genet. 26, 29-50
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 29-50
    • Kurland, C.G.1
  • 10
    • 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. U.S.A. 108, 6933-6938
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6933-6938
    • Jones, T.E.1    Alexander, R.W.2    Pan, T.3
  • 12
    • 84887575499 scopus 로고    scopus 로고
    • G/U and certain wobble position mismatches as possible main causes of amino acid misincorporations
    • Zhang, Z., Shah, B., and Bondarenko, P. V. (2013) G/U and certain wobble position mismatches as possible main causes of amino acid misincorporations. Biochemistry 52, 8165-8176
    • (2013) Biochemistry , vol.52 , pp. 8165-8176
    • Zhang, Z.1    Shah, B.2    Bondarenko, P.V.3
  • 13
    • 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. U.S.A. 85, 1033-1037
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 14
    • 0141957401 scopus 로고    scopus 로고
    • Activation of the pyrrolysine suppressor tRNA requires formation of a ternary complex with class I and class II Lysyl-tRNA synthetases
    • DOI 10.1016/S1097-2765(03)00280-6
    • Polycarpo, C., Ambrogelly, A., Ruan, B., Tumbula-Hansen, D., Ataide, S. F., Ishitani, R., Yokoyama, S., Nureki, O., Ibba, M., and Söll, D. (2003) Activation of the pyrrolysine suppressor tRNA requires formation of a ternary complex with class I and class II lysyl-tRNA synthetases. Mol. Cell 12, 287-294 (Pubitemid 37238916)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 287-294
    • Polycarpo, C.1    Ambrogelly, A.2    Ruan, B.3    Tumbula-Hansen, D.4    Ataide, S.F.5    Ishitani, R.6    Yokoyama, S.7    Nureki, O.8    Ibba, M.9    Soll, D.10
  • 15
    • 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 β 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
  • 16
    • 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
  • 17
    • 38649136232 scopus 로고    scopus 로고
    • Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases
    • DOI 10.1016/j.ymeth.2007.09.007, PII S1046202307001727
    • Francklyn, C. S., First, E. A., Perona, J. J., and Hou, Y. M. (2008) Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases. Methods 44, 100-118 (Pubitemid 351172808)
    • (2008) Methods , vol.44 , Issue.2 , pp. 100-118
    • Francklyn, C.S.1    First, E.A.2    Perona, J.J.3    Hou, Y.-M.4
  • 18
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • DOI 10.1093/nar/25.5.955
    • Lowe, T. M., and Eddy, S. R. (1997) tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res. 25, 955-964 (Pubitemid 27298263)
    • (1997) Nucleic Acids Research , vol.25 , Issue.5 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 19
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • DOI 10.1126/science.284.5411.147
    • Wakasugi, K., and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284, 147-151 (Pubitemid 29282068)
    • (1999) Science , vol.284 , Issue.5411 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 20
    • 0030945598 scopus 로고    scopus 로고
    • Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine
    • DOI 10.1074/jbc.272.22.14420
    • Kleeman, T. A., Wei, D., Simpson, K. L., and First, E. A. (1997) Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J. Biol. Chem. 272, 14420-14425 (Pubitemid 27232860)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14420-14425
    • Kleeman, T.A.1    Wei, D.2    Simpson, K.L.3    First, E.A.4
  • 21
    • 0037036396 scopus 로고    scopus 로고
    • Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase
    • DOI 10.1074/jbc.M201923200
    • Austin, J., and First, E. A. (2002) Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase. J. Biol. Chem. 277, 20243-20248 (Pubitemid 34967316)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20243-20248
    • Austin, J.1    First, E.A.2
  • 22
    • 0023110653 scopus 로고
    • Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine
    • DOI 10.1016/0022-2836(87)90376-7
    • Brick, P., and Blow, D. M. (1987) Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. J. Mol. Biol. 194, 287-297 (Pubitemid 17044524)
    • (1987) Journal of Molecular Biology , vol.194 , Issue.2 , pp. 287-297
    • Brick, P.1    Blow, D.M.2
  • 23
    • 0024722501 scopus 로고
    • Errors and alternatives in reading the universal genetic code
    • Parker, J. (1989) Errors and alternatives in reading the universal genetic code. Microbiol. Rev. 53, 273-298
    • (1989) Microbiol. Rev. , vol.53 , pp. 273-298
    • Parker, J.1
  • 24
    • 70450253191 scopus 로고    scopus 로고
    • Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells
    • Wen, D., Vecchi, M. M., Gu, S., Su, L., Dolnikova, J., Huang, Y. M., Foley, S. F., Garber, E., Pederson, N., and Meier, W. (2009) Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells. J. Biol. Chem. 284, 32686-32694
    • (2009) J. Biol. Chem. , vol.284 , pp. 32686-32694
    • Wen, D.1    Vecchi, M.M.2    Gu, S.3    Su, L.4    Dolnikova, J.5    Huang, Y.M.6    Foley, S.F.7    Garber, E.8    Pederson, N.9    Meier, W.10
  • 25
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling, J., and Söll, D. (2010) Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc. Natl. Acad. Sci. U.S.A. 107, 4028-4033
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4028-4033
    • Ling, J.1    Söll, D.2
  • 26
    • 0030568996 scopus 로고    scopus 로고
    • High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli
    • DOI 10.1006/jmbi.1996.0524
    • Calderone, T. L., Stevens, R. D., and Oas, T. G. (1996) High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli. J. Mol. Biol. 262, 407-412 (Pubitemid 26341163)
    • (1996) Journal of Molecular Biology , vol.262 , Issue.4 , pp. 407-412
    • Calderone, T.L.1    Stevens, R.D.2    Oas, T.G.3
  • 27
    • 70649100426 scopus 로고    scopus 로고
    • Identification of codon-specific serine to asparagine mistranslation in recombinant monoclonal antibodies by high-resolution mass spectrometry
    • Yu, X. C., Borisov, O. V., Alvarez, M., Michels, D. A., Wang, Y. J., and Ling, V. (2009) Identification of codon-specific serine to asparagine mistranslation in recombinant monoclonal antibodies by high-resolution mass spectrometry. Anal. Chem. 81, 9282-9290
    • (2009) Anal. Chem. , vol.81 , pp. 9282-9290
    • Yu, X.C.1    Borisov, O.V.2    Alvarez, M.3    Michels, D.A.4    Wang, Y.J.5    Ling, V.6
  • 28
    • 0027445423 scopus 로고
    • Assessing genetic heterogeneity in production cell lines: Detection by peptide mapping of a low level Tyr to Gln sequence variant in a recombinant antibody
    • Harris, R. J., Murnane, A. A., Utter, S. L., Wagner, K. L., Cox, E. T., Polastri, G. D., Helder, J. C., and Sliwkowski, M. B. (1993) Assessing genetic heterogeneity in production cell lines: detection by peptide mapping of a low level Tyr to Gln sequence variant in a recombinant antibody. Biotechnology 11, 1293-1297
    • (1993) Biotechnology , vol.11 , pp. 1293-1297
    • Harris, R.J.1    Murnane, A.A.2    Utter, S.L.3    Wagner, K.L.4    Cox, E.T.5    Polastri, G.D.6    Helder, J.C.7    Sliwkowski, M.B.8
  • 29
    • 0030271498 scopus 로고    scopus 로고
    • Errors of heterologous protein expression
    • DOI 10.1016/S0958-1669(96)80050-4
    • Kurland, C., and Gallant, J. (1996) Errors of heterologous protein expression. Curr. Opin. Biotechnol. 7, 489-493 (Pubitemid 26381749)
    • (1996) Current Opinion in Biotechnology , vol.7 , Issue.5 , pp. 489-493
    • Kurland, C.1    Gallant, J.2
  • 30
    • 70349333227 scopus 로고    scopus 로고
    • The evolutionary consequences of erroneous protein synthesis
    • Drummond, D. A., and Wilke, C. O. (2009) The evolutionary consequences of erroneous protein synthesis. Nat. Rev. Genet. 10, 715-724
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 715-724
    • Drummond, D.A.1    Wilke, C.O.2
  • 33
    • 0019830818 scopus 로고
    • Enzymic editing mechanisms and the genetic code
    • Fersht, A. R. (1981) Enzymic editing mechanisms and the genetic code. Proc. R Soc. Lond. B Biol. Sci. 212, 351-379
    • (1981) Proc. R Soc. Lond. B Biol. Sci. , vol.212 , pp. 351-379
    • Fersht, A.R.1
  • 34
    • 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
  • 36
    • 17744373680 scopus 로고    scopus 로고
    • Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine
    • DOI 10.1110/ps.041239305
    • Zhang, Y., Wang, L., Schultz, P. G., and Wilson, I. A. (2005) Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine. Protein Sci. 14, 1340-1349 (Pubitemid 40577813)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1340-1349
    • Zhang, Y.1    Wang, L.2    Schultz, P.G.3    Wilson, I.A.4
  • 37
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues
    • Oue, S., Okamoto, A., Yano, T., and Kagamiyama, H. (1999) Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J. Biol. Chem. 274, 2344-2349
    • (1999) J. Biol. Chem. , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4


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