메뉴 건너뛰기




Volumn 4, Issue 2, 2013, Pages

Divergent protein motifs direct elongation factor P-mediated translational regulation in salmonella enterica and Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; ELONGATION FACTOR; ELONGATION FACTOR P; POXB PROTEIN; PROLINE; PROTEOME; TRIPEPTIDE; UNCLASSIFIED DRUG; FACTOR EF P; FACTOR EF-P;

EID: 84880064840     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00180-13     Document Type: Article
Times cited : (76)

References (47)
  • 2
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa H, Ito K. 2002. The ribosomal exit tunnel functions as a discriminating gate. Cell 108:629-636.
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 3
    • 4344668509 scopus 로고    scopus 로고
    • Translation arrest of SecM is essential for the basal and regulated expression of SecA
    • Murakami A, Nakatogawa H, Ito K. 2004. Translation arrest of SecM is essential for the basal and regulated expression of SecA. Proc. Natl. Acad. Sci. U. S. A. 101:12330-12335.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 12330-12335
    • Murakami, A.1    Nakatogawa, H.2    Ito, K.3
  • 4
    • 0035105116 scopus 로고    scopus 로고
    • Secretion monitor, SecM, undergoes selftranslation arrest in the cytosol
    • Nakatogawa H, Ito K. 2001. Secretion monitor, SecM, undergoes selftranslation arrest in the cytosol. Mol. Cell 7:185-192.
    • (2001) Mol. Cell , vol.7 , pp. 185-192
    • Nakatogawa, H.1    Ito, K.2
  • 6
    • 84860231100 scopus 로고    scopus 로고
    • The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria
    • Li GW, Oh E, Weissman JS. 2012. The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria. Nature 484: 538-541.
    • (2012) Nature , vol.484 , pp. 538-541
    • Li, G.W.1    Oh, E.2    Weissman, J.S.3
  • 7
    • 79251557798 scopus 로고    scopus 로고
    • Nascent peptide in the ribosome exit tunnel affects functional properties of the A-site of the peptidyl transferase center
    • Ramu H, Vázquez-Laslop N, Klepacki D, Dai Q, Piccirilli J, Micura R, Mankin AS. 2011. Nascent peptide in the ribosome exit tunnel affects functional properties of the A-site of the peptidyl transferase center. Mol. Cell 41:321-330.
    • (2011) Mol. Cell , vol.41 , pp. 321-330
    • Ramu, H.1    Vázquez-Laslop, N.2    Klepacki, D.3    Dai, Q.4    Piccirilli, J.5    Micura, R.6    Mankin, A.S.7
  • 8
    • 1242273896 scopus 로고    scopus 로고
    • Nascentpeptide- mediated ribosome stalling at a stop codon induces mRNA cleavage resulting in nonstop mRNA that is recognized by tmRNA
    • Sunohara T, Jojima K, Yamamoto Y, Inada T, Aiba H. 2004. Nascentpeptide- mediated ribosome stalling at a stop codon induces mRNA cleavage resulting in nonstop mRNA that is recognized by tmRNA. RNA 10: 378-386.
    • (2004) RNA , vol.10 , pp. 378-386
    • Sunohara, T.1    Jojima, K.2    Yamamoto, Y.3    Inada, T.4    Aiba, H.5
  • 10
    • 79957631259 scopus 로고    scopus 로고
    • A mutation in the poxA gene of Salmonella enterica serovar typhimurium alters protein production, elevates susceptibility to environmental challenges, and decreases swine colonization
    • Bearson SM, Bearson BL, Brunelle BW, Sharma VK, Lee IS. 2011. A mutation in the poxA gene of Salmonella enterica serovar typhimurium alters protein production, elevates susceptibility to environmental challenges, and decreases swine colonization. Foodborne Pathog. Dis. 8:725-732.
    • (2011) Foodborne Pathog. Dis , vol.8 , pp. 725-732
    • Bearson, S.M.1    Bearson, B.L.2    Brunelle, B.W.3    Sharma, V.K.4    Lee, I.S.5
  • 12
    • 0023548410 scopus 로고
    • Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity
    • Van Dyk TK, Smulski DR, Chang YY. 1987. Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity. J. Bacteriol. 169:4540-4546.
    • (1987) J. Bacteriol , vol.169 , pp. 4540-4546
    • van Dyk, T.K.1    Smulski, D.R.2    Chang, Y.Y.3
  • 16
    • 0035190137 scopus 로고    scopus 로고
    • The chvH locus of Agrobacterium encodes a homologue of an elongation factor involved in protein synthesis
    • Peng WT, Banta LM, Charles TC, Nester EW. 2001. The chvH locus of Agrobacterium encodes a homologue of an elongation factor involved in protein synthesis. J. Bacteriol. 183:36-45.
    • (2001) J. Bacteriol , vol.183 , pp. 36-45
    • Peng, W.T.1    Banta, L.M.2    Charles, T.C.3    Nester, E.W.4
  • 17
    • 84871921644 scopus 로고    scopus 로고
    • EF-P is essential for rapid synthesis of proteins containing consecutive proline residues
    • Doerfel LK, Wohlgemuth I, Kothe C, Peske F, Urlaub H, Rodnina MV. 2013. EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339:85-88.
    • (2013) Science , vol.339 , pp. 85-88
    • Doerfel, L.K.1    Wohlgemuth, I.2    Kothe, C.3    Peske, F.4    Urlaub, H.5    Rodnina, M.V.6
  • 18
    • 84871918588 scopus 로고    scopus 로고
    • Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches
    • Ude S, Lassak J, Starosta AL, Kraxenberger T, Wilson DN, Jung K. 2013. Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science 339:82-85.
    • (2013) Science , vol.339 , pp. 82-85
    • Ude, S.1    Lassak, J.2    Starosta, A.L.3    Kraxenberger, T.4    Wilson, D.N.5    Jung, K.6
  • 19
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1:376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 20
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong SE, Foster LJ, Mann M. 2003. Mass spectrometric-based approaches in quantitative proteomics. Methods 29:124-130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 21
    • 0020419588 scopus 로고
    • Mapping nonselectable genes of Escherichia coli by using transposon Tn10: Location of a gene affecting pyruvate oxidase
    • Chang YY, Cronan JE, Jr. 1982. Mapping nonselectable genes of Escherichia coli by using transposon Tn10: location of a gene affecting pyruvate oxidase. J. Bacteriol. 151:1279-1289.
    • (1982) J. Bacteriol , vol.151 , pp. 1279-1289
    • Chang, Y.Y.1    Cronan Jr., J.E.2
  • 23
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang DW, Sherman BT, Lempicki RA. 2009. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37:1-13.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 24
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang DW, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4:44-57.
    • (2009) Nat. Protoc , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 25
    • 84864523802 scopus 로고    scopus 로고
    • Structural basis for intersubunit signaling in a protein disaggregating machine
    • Biter AB, Lee S, Sung N, Tsai FT. 2012. Structural basis for intersubunit signaling in a protein disaggregating machine. Proc. Natl. Acad. Sci. U. S. A. 109:12515-12520.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 12515-12520
    • Biter, A.B.1    Lee, S.2    Sung, N.3    Tsai, F.T.4
  • 26
    • 84863959033 scopus 로고    scopus 로고
    • Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
    • Rees DM, Montgomery MG, Leslie AG, Walker JE. 2012. Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria. Proc. Natl. Acad. Sci. U. S. A. 109:11139-11143.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 11139-11143
    • Rees, D.M.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 27
    • 0036773132 scopus 로고    scopus 로고
    • Hexameric ring structure of the ATPase domain of the membraneintegrated metalloprotease FtsH from Thermus thermophilus HB8
    • Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K. 2002. Hexameric ring structure of the ATPase domain of the membraneintegrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 10:1415-1423.
    • (2002) Structure , vol.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 29
    • 0020532234 scopus 로고
    • Genetic and biochemical analyses of Escherichia coli strains having a mutation in the structural gene (poxB) for pyruvate oxidase
    • Chang YY, Cronan JE, Jr. 1983. Genetic and biochemical analyses of Escherichia coli strains having a mutation in the structural gene (poxB) for pyruvate oxidase. J. Bacteriol. 154:756-762.
    • (1983) J. Bacteriol , vol.154 , pp. 756-762
    • Chang, Y.Y.1    Cronan Jr., J.E.2
  • 30
    • 84866857051 scopus 로고    scopus 로고
    • Multisite ribosomal stalling: A unique mode of regulatory nascent chain action revealed for MifM
    • Chiba S, Ito K. 2012. Multisite ribosomal stalling: a unique mode of regulatory nascent chain action revealed for MifM. Mol. Cell 47:863-872.
    • (2012) Mol. Cell , vol.47 , pp. 863-872
    • Chiba, S.1    Ito, K.2
  • 31
    • 0037072627 scopus 로고    scopus 로고
    • Instruction of translating ribosome by nascent peptide
    • Gong F, Yanofsky C. 2002. Instruction of translating ribosome by nascent peptide. Science 297:1864-1867.
    • (2002) Science , vol.297 , pp. 1864-1867
    • Gong, F.1    Yanofsky, C.2
  • 32
    • 0024404852 scopus 로고
    • Erythromycin-induced ribosome stall in the ermA leader: A barricade to 5=-to-3= nucleolytic cleavage of the ermA transcript
    • Sandler P, Weisblum B. 1989. Erythromycin-induced ribosome stall in the ermA leader: a barricade to 5=-to-3= nucleolytic cleavage of the ermA transcript. J. Bacteriol. 171:6680-6688.
    • (1989) J. Bacteriol , vol.171 , pp. 6680-6688
    • Sandler, P.1    Weisblum, B.2
  • 33
    • 77649251845 scopus 로고    scopus 로고
    • Structural and biochemical characterization of SrcA, a multi-cargo type III secretion chaperone in Salmonella required for pathogenic association with a host
    • Cooper CA, Zhang K, Andres SN, Fang Y, Kaniuk NA, Hannemann M, Brumell JH, Foster LJ, Junop MS, Coombes BK. 2010. Structural and biochemical characterization of SrcA, a multi-cargo type III secretion chaperone in Salmonella required for pathogenic association with a host. PLoS Pathog. 6:e1000751. http://dx.doi.org/10.1371/journal.ppat.1000751.
    • (2010) PLoS Pathog , vol.6
    • Cooper, C.A.1    Zhang, K.2    Andres, S.N.3    Fang, Y.4    Kaniuk, N.A.5    Hannemann, M.6    Brumell, J.H.7    Foster, L.J.8    Junop, M.S.9    Coombes, B.K.10
  • 34
    • 0014992845 scopus 로고
    • A method for detection of phage mutants with altered transducing ability
    • Schmieger H. 1971. A method for detection of phage mutants with altered transducing ability. Mol. Gen. Genet. 110:378-381.
    • (1971) Mol. Gen. Genet , vol.110 , pp. 378-381
    • Schmieger, H.1
  • 36
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 37
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 38
    • 84859988230 scopus 로고    scopus 로고
    • Superfolder GFP reporters validate diverse new mRNA targets of the classic porin regulator, MicF RNA
    • Corcoran CP, Podkaminski D, Papenfort K, Urban JH, Hinton JC, Vogel J. 2012. Superfolder GFP reporters validate diverse new mRNA targets of the classic porin regulator, MicF RNA. Mol. Microbiol. 84: 428-445.
    • (2012) Mol. Microbiol , vol.84 , pp. 428-445
    • Corcoran, C.P.1    Podkaminski, D.2    Papenfort, K.3    Urban, J.H.4    Hinton, J.C.5    Vogel, J.6
  • 40
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY. 2004. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22:1567-1572.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 41
    • 0023762645 scopus 로고
    • Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity
    • Sharp PM, Cowe E, Higgins DG, Shields DC, Wolfe KH, Wright F. 1988. Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity. Nucleic Acids Res. 16:8207-8211.
    • (1988) Nucleic Acids Res , vol.16 , pp. 8207-8211
    • Sharp, P.M.1    Cowe, E.2    Higgins, D.G.3    Shields, D.C.4    Wolfe, K.H.5    Wright, F.6
  • 42
    • 85011940605 scopus 로고    scopus 로고
    • Elongation factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence
    • Zou SB, Roy H, Ibba M, Navarre WW. 2011. Elongation factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence. Virulence 2:147-151.
    • (2011) Virulence , vol.2 , pp. 147-151
    • Zou, S.B.1    Roy, H.2    Ibba, M.3    Navarre, W.W.4
  • 43
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 44
    • 33845973020 scopus 로고    scopus 로고
    • Quantitative comparison of caste differences in honeybee hemolymph
    • Chan QW, Howes CG, Foster LJ. 2006. Quantitative comparison of caste differences in honeybee hemolymph. Mol. Cell. Proteomics 5:2252-2262.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2252-2262
    • Chan, Q.W.1    Howes, C.G.2    Foster, L.J.3
  • 46
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for datadriven systems biology
    • Cox J, Mann M. 2011. Quantitative, high-resolution proteomics for datadriven systems biology. Annu. Rev. Biochem. 80:273-299.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.