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Volumn 6, Issue 6, 2011, Pages

A ribosomal misincorporation of lys for arg in human triosephosphate isomerase expressed in escherichia coli gives rise to two protein populations

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CELL PROTEIN; ISOLEUCINE; LEUCINE; LYSINE; PROTEIN P1; PROTEIN P2; PROTEINASE K; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; UREA;

EID: 79959595380     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021035     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 0021092735 scopus 로고
    • Codon-specific missense errors in vivo
    • Bouadloun F, Donner D, Kurland CG, (1983) Codon-specific missense errors in vivo. EMBO J 2: 1351-1356.
    • (1983) EMBO J , vol.2 , pp. 1351-1356
    • Bouadloun, F.1    Donner, D.2    Kurland, C.G.3
  • 2
    • 0017610661 scopus 로고
    • Mistranslation in E. coli
    • Edelmann P, Gallant J, (1977) Mistranslation in E. coli. Cell 10: 131-137.
    • (1977) Cell , vol.10 , pp. 131-137
    • Edelmann, P.1    Gallant, J.2
  • 3
    • 33845895536 scopus 로고    scopus 로고
    • The frequency of translational misreading errors in E. coli is largely determined by tRNA competition
    • Kramer EB, Farabaugh PJ, (2007) The frequency of translational misreading errors in E. coli is largely determined by tRNA competition. RNA 13: 87-96.
    • (2007) RNA , vol.13 , pp. 87-96
    • Kramer, E.B.1    Farabaugh, P.J.2
  • 4
    • 77956019364 scopus 로고    scopus 로고
    • A comprehensive analysis of translational missense errors in the yeast Saccharomyces cerevisiae
    • Kramer EB, Vallabhaneni H, Mayer LM, Farabaugh PJ, (2010) A comprehensive analysis of translational missense errors in the yeast Saccharomyces cerevisiae. RNA 16: 1797-1808.
    • (2010) RNA , vol.16 , pp. 1797-1808
    • Kramer, E.B.1    Vallabhaneni, H.2    Mayer, L.M.3    Farabaugh, P.J.4
  • 5
    • 0023658021 scopus 로고
    • Mistranslation in twelve Escherichia coli ribosomal proteins. Cysteine misincorporation at neutral amino acid residues other than tryptophan
    • Laughrea M, Latulippe J, Filion AM, Boulet L, (1987) Mistranslation in twelve Escherichia coli ribosomal proteins. Cysteine misincorporation at neutral amino acid residues other than tryptophan. Eur J Biochem 169: 59-64.
    • (1987) Eur J Biochem , vol.169 , pp. 59-64
    • Laughrea, M.1    Latulippe, J.2    Filion, A.M.3    Boulet, L.4
  • 6
    • 70349333227 scopus 로고    scopus 로고
    • The evolutionary consequences of erroneous protein synthesis
    • Drummond DA, Wilke CO, (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
  • 7
    • 47549108636 scopus 로고    scopus 로고
    • Costly mistakes: translational infidelity and protein homeostasis
    • Powers ET, Balch WE, (2008) Costly mistakes: translational infidelity and protein homeostasis. Cell 134: 204-206.
    • (2008) Cell , vol.134 , pp. 204-206
    • Powers, E.T.1    Balch, W.E.2
  • 9
    • 65549084298 scopus 로고    scopus 로고
    • Potential role of phenotypic mutations in the evolution of protein expression and stability
    • Goldsmith M, Tawfik DS, (2009) Potential role of phenotypic mutations in the evolution of protein expression and stability. Proc Natl Acad Sci U S A 106: 6197-6202.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6197-6202
    • Goldsmith, M.1    Tawfik, D.S.2
  • 10
    • 71549165759 scopus 로고    scopus 로고
    • Genetic code ambiguity: an unexpected source of proteome innovation and phenotypic diversity
    • Moura GR, Carreto LC, Santos MA, (2009) Genetic code ambiguity: an unexpected source of proteome innovation and phenotypic diversity. Curr Opin Microbiol 12: 631-637.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 631-637
    • Moura, G.R.1    Carreto, L.C.2    Santos, M.A.3
  • 11
    • 77954918654 scopus 로고    scopus 로고
    • Visualizing high error levels during gene expression in living bacterial cells
    • Meyerovich M, Mamou G, Ben-Yehuda S, (2010) Visualizing high error levels during gene expression in living bacterial cells. Proc Natl Acad Sci U S A 107: 11543-11548.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11543-11548
    • Meyerovich, M.1    Mamou, G.2    Ben-Yehuda, S.3
  • 12
    • 78650304100 scopus 로고    scopus 로고
    • Synonymous but not the same: the causes and consequences of codon bias
    • Plotkin JB, Kudla G, (2011) Synonymous but not the same: the causes and consequences of codon bias. Nat Rev Genet 12: 32-42.
    • (2011) Nat Rev Genet , vol.12 , pp. 32-42
    • Plotkin, J.B.1    Kudla, G.2
  • 13
    • 0024284374 scopus 로고
    • Codon preference reflects mistranslational constraints: a proposal
    • McPherson DT, (1988) Codon preference reflects mistranslational constraints: a proposal. Nucleic Acids Res 16: 4111-4120.
    • (1988) Nucleic Acids Res , vol.16 , pp. 4111-4120
    • McPherson, D.T.1
  • 14
    • 0031662136 scopus 로고    scopus 로고
    • The genetic code is one in a million
    • Freeland SJ, Hurst LD, (1998) The genetic code is one in a million. J Mol Evol 47: 238-248.
    • (1998) J Mol Evol , vol.47 , pp. 238-248
    • Freeland, S.J.1    Hurst, L.D.2
  • 15
    • 20244377336 scopus 로고
    • Mistranslation in IGF-1 during over-expression of the protein in Escherichia coli using a synthetic gene containing low frequency codons
    • Seetharam R, Heeren RA, Wong EY, Braford SR, Klein BK, et al. (1988) Mistranslation in IGF-1 during over-expression of the protein in Escherichia coli using a synthetic gene containing low frequency codons. Biochem Biophys Res Commun 155: 518-523.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 518-523
    • Seetharam, R.1    Heeren, R.A.2    Wong, E.Y.3    Braford, S.R.4    Klein, B.K.5
  • 16
    • 0030568996 scopus 로고    scopus 로고
    • High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli
    • Calderone TL, Stevens RD, Oas TG, (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.
    • (1996) J Mol Biol , vol.262 , pp. 407-412
    • Calderone, T.L.1    Stevens, R.D.2    Oas, T.G.3
  • 17
    • 0030221293 scopus 로고    scopus 로고
    • Overexpression, purification, and refolding of link module from human TSG-6 in Escherichia coli: effect of temperature, media, and mutagenesis on lysine misincorporation at arginine AGA codons
    • Day AJ, Aplin RT, Willis AC, (1996) Overexpression, purification, and refolding of link module from human TSG-6 in Escherichia coli: effect of temperature, media, and mutagenesis on lysine misincorporation at arginine AGA codons. Protein Expr Purif 8: 1-16.
    • (1996) Protein Expr Purif , vol.8 , pp. 1-16
    • Day, A.J.1    Aplin, R.T.2    Willis, A.C.3
  • 18
    • 0031938042 scopus 로고    scopus 로고
    • High level, context dependent misincorporation of lysine for arginine in Saccharomyces cerevisiae a1 homeodomain expressed in Escherichia coli
    • Forman MD, Stack RF, Masters PS, Hauer CR, Baxter SM, (1998) High level, context dependent misincorporation of lysine for arginine in Saccharomyces cerevisiae a1 homeodomain expressed in Escherichia coli. Protein Sci 7: 500-503.
    • (1998) Protein Sci , vol.7 , pp. 500-503
    • Forman, M.D.1    Stack, R.F.2    Masters, P.S.3    Hauer, C.R.4    Baxter, S.M.5
  • 19
    • 53149132027 scopus 로고    scopus 로고
    • Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface
    • Rodriguez-Almazan C, Arreola R, Rodriguez-Larrea D, Aguirre-Lopez B, de Gomez-Puyou MT, et al. (2008) Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem 283: 23254-23263.
    • (2008) J Biol Chem , vol.283 , pp. 23254-23263
    • Rodriguez-Almazan, C.1    Arreola, R.2    Rodriguez-Larrea, D.3    Aguirre-Lopez, B.4    de Gomez-Puyou, M.T.5
  • 20
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y, Gojobori T, Ikemura T, (2000) Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acids Res 28: 292.
    • (2000) Nucleic Acids Res , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 21
    • 0036134273 scopus 로고    scopus 로고
    • Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis
    • Wang W, Malcolm BA, (2002) Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis. Methods Mol Biol 182: 37-43.
    • (2002) Methods Mol Biol , vol.182 , pp. 37-43
    • Wang, W.1    Malcolm, B.A.2
  • 22
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS, (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8: 1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 23
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T, (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 24
    • 0003689123 scopus 로고    scopus 로고
    • Protein Sequencing and Identification Using Tandem Mass Spectrometry
    • Wiley Interscience, New York
    • Kinter M, Sherman N, (2000) Protein Sequencing and Identification Using Tandem Mass Spectrometry. Wiley Interscience, New York.
    • (2000)
    • Kinter, M.1    Sherman, N.2
  • 25
    • 79959622765 scopus 로고    scopus 로고
    • Varsplic utility and alternative isoform files
    • Available via; last accessed 12/8/10
    • Varsplic utility and alternative isoform files. Available via ftp://ftp.expasy.org/databases/uniprot/knowledgebase/README.varsplic; last accessed 12/8/10.
  • 26
    • 84871237658 scopus 로고    scopus 로고
    • Uniprot website
    • Available at; last accessed 1/11/11
    • Uniprot website. Available at http://www.uniprot.org/news/2010/11/30/release; last accessed 1/11/11.
  • 27
    • 79959598348 scopus 로고    scopus 로고
    • A Perl module for creating and parsing SwissProt files
    • Swissknife, Available at; last accessed 12/8/10. "Sequence Database Setup: Utilities"
    • Swissknife A Perl module for creating and parsing SwissProt files. Available at ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/; last accessed 12/8/10. "Sequence Database Setup: Utilities".
  • 28
    • 84947650183 scopus 로고    scopus 로고
    • Matrix Science website
    • Sequence Database Setup: Utilities available at; last accessed 12/8/10
    • Matrix Science website. Sequence Database Setup: Utilities available at http://www.matrixscience.com/help/seq_db_setup.html; last accessed 12/8/10.
  • 29
    • 77951952886 scopus 로고    scopus 로고
    • Easy retrieval of single amino-acid polymorphisms and phenotype information using SwissVar
    • Mottaz A, David FP, Veuthey AL, Yip YL, (2010) Easy retrieval of single amino-acid polymorphisms and phenotype information using SwissVar. Bioinformatics 26: 851-852.
    • (2010) Bioinformatics , vol.26 , pp. 851-852
    • Mottaz, A.1    David, F.P.2    Veuthey, A.L.3    Yip, Y.L.4
  • 30
    • 54049151142 scopus 로고    scopus 로고
    • Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia
    • Hernandez-Alcantara G, Rodriguez-Romero A, Reyes-Vivas H, Peon J, Cabrera N, et al. (2008) Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia. Biochim Biophys Acta 1784: 1493-1500.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1493-1500
    • Hernandez-Alcantara, G.1    Rodriguez-Romero, A.2    Reyes-Vivas, H.3    Peon, J.4    Cabrera, N.5
  • 31
    • 77954002740 scopus 로고    scopus 로고
    • Gene optimization mechanisms: a multi-gene study reveals a high success rate of full-length human proteins expressed in Escherichia coli
    • Maertens B, Spriestersbach A, von Groll U, Roth U, Kubicek J, et al. (2010) Gene optimization mechanisms: a multi-gene study reveals a high success rate of full-length human proteins expressed in Escherichia coli. Protein Sci 19: 1312-1326.
    • (2010) Protein Sci , vol.19 , pp. 1312-1326
    • Maertens, B.1    Spriestersbach, A.2    von Groll, U.3    Roth, U.4    Kubicek, J.5
  • 32
    • 48249093081 scopus 로고    scopus 로고
    • Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host
    • Angov E, Hillier CJ, Kincaid RL, Lyon JA, (2008) Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host. PLoS One 3: e2189.
    • (2008) PLoS One , vol.3
    • Angov, E.1    Hillier, C.J.2    Kincaid, R.L.3    Lyon, J.A.4
  • 33
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane JF, (1995) Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr Opin Biotechnol 6: 494-500.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 34
    • 0030271498 scopus 로고    scopus 로고
    • Errors of heterologous protein expression
    • Kurland C, Gallant J, (1996) Errors of heterologous protein expression. Curr Opin Biotechnol 7: 489-493.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 489-493
    • Kurland, C.1    Gallant, J.2
  • 35
    • 14644396660 scopus 로고    scopus 로고
    • Selective charging of tRNA isoacceptors induced by amino-acid starvation
    • Dittmar KA, Sorensen MA, Elf J, Ehrenberg M, Pan T, (2005) Selective charging of tRNA isoacceptors induced by amino-acid starvation. EMBO Rep 6: 151-157.
    • (2005) EMBO Rep , vol.6 , pp. 151-157
    • Dittmar, K.A.1    Sorensen, M.A.2    Elf, J.3    Ehrenberg, M.4    Pan, T.5
  • 36
    • 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
  • 37
    • 44649171519 scopus 로고    scopus 로고
    • New features of the ribosome and ribosomal inhibitors: non-enzymatic recycling, misreading and back-translocation
    • Szaflarski W, Vesper O, Teraoka Y, Plitta B, Wilson DN, et al. (2008) New features of the ribosome and ribosomal inhibitors: non-enzymatic recycling, misreading and back-translocation. J Mol Biol 380: 193-205.
    • (2008) J Mol Biol , vol.380 , pp. 193-205
    • Szaflarski, W.1    Vesper, O.2    Teraoka, Y.3    Plitta, B.4    Wilson, D.N.5
  • 38
    • 70649100426 scopus 로고    scopus 로고
    • Identification of codon-specific serine to asparagine mistranslation in recombinant monoclonal antibodies by high-resolution mass spectrometry
    • Yu XC, Borisov OV, Alvarez M, Michels DA, Wang YJ, et al. (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
  • 40
    • 64049115856 scopus 로고    scopus 로고
    • Bases in the anticodon loop of tRNA(Ala)(GGC) prevent misreading
    • Murakami H, Ohta A, Suga H, (2009) Bases in the anticodon loop of tRNA(Ala)(GGC) prevent misreading. Nat Struct Mol Biol 16: 353-358.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 353-358
    • Murakami, H.1    Ohta, A.2    Suga, H.3
  • 41
    • 64049100740 scopus 로고    scopus 로고
    • A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding
    • Ledoux S, Olejniczak M, Uhlenbeck OC, (2009) A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding. Nat Struct Mol Biol 16: 359-364.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 359-364
    • Ledoux, S.1    Olejniczak, M.2    Uhlenbeck, O.C.3
  • 42
  • 43
    • 39149086991 scopus 로고    scopus 로고
    • A genetic code alteration generates a proteome of high diversity in the human pathogen Candida albicans
    • Gomes AC, Miranda I, Silva RM, Moura GR, Thomas B, et al. (2007) A genetic code alteration generates a proteome of high diversity in the human pathogen Candida albicans. Genome Biol 8: R206.
    • (2007) Genome Biol , vol.8
    • Gomes, A.C.1    Miranda, I.2    Silva, R.M.3    Moura, G.R.4    Thomas, B.5
  • 45
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures
    • Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, et al. (1999) The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins 37: 441-453.
    • (1999) Proteins , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3    Beaucamp, N.4    Alvarez, M.5
  • 48
    • 0033080755 scopus 로고    scopus 로고
    • Spontaneous alpha-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins
    • Geoghegan KF, Dixon HB, Rosner PJ, Hoth LR, Lanzetti AJ, et al. (1999) Spontaneous alpha-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267: 169-184.
    • (1999) Anal Biochem , vol.267 , pp. 169-184
    • Geoghegan, K.F.1    Dixon, H.B.2    Rosner, P.J.3    Hoth, L.R.4    Lanzetti, A.J.5
  • 49
    • 0013784519 scopus 로고
    • Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups
    • Stark GR, (1965) Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups. Biochemistry 4: 1030-1036.
    • (1965) Biochemistry , vol.4 , pp. 1030-1036
    • Stark, G.R.1


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