메뉴 건너뛰기




Volumn 338, Issue 1, 2004, Pages 33-41

Ribosome rescue by tmRNA requires truncated mRNAs

Author keywords

ORF, open reading frame; Protein synthesis; RC, ribosome complex; Ribosome; SD, Shine Dalgarno; tmRNA; trans translation kinetics

Indexed keywords

MESSENGER RNA; RNA;

EID: 1842526451     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.043     Document Type: Article
Times cited : (104)

References (34)
  • 1
    • 0035985042 scopus 로고    scopus 로고
    • SsrA-mediated protein tagging in the presence of miscoding drugs and its physiological role in Escherichia coli
    • Abo T., Ueda K., Sunohara T., Ogawa K., Aiba H. SsrA-mediated protein tagging in the presence of miscoding drugs and its physiological role in Escherichia coli. Genes Cells. 7:2002;629-638.
    • (2002) Genes Cells , vol.7 , pp. 629-638
    • Abo, T.1    Ueda, K.2    Sunohara, T.3    Ogawa, K.4    Aiba, H.5
  • 2
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev L., Ehrenberg M., Frolova L. Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 22:2003;175-182.
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.3
  • 3
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi R., Pavlov M.Y., Buckingham R.H., Ehrenberg M. Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell. 3:1999;601-609.
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 4
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal a site
    • Pedersen K., Zavialov A.V., Pavlov M.Y., Elf J., Gerdes K., Ehrenberg M. The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell. 112:2003;131-140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 5
    • 0030026177 scopus 로고    scopus 로고
    • A case for trans translation
    • Atkins J.F., Gesteland R.F. A case for trans translation. Nature. 379:1996;769-771.
    • (1996) Nature , vol.379 , pp. 769-771
    • Atkins, J.F.1    Gesteland, R.F.2
  • 6
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler K.C., Waller P.R., Sauer R.T. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science. 271:1996;990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 7
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • Karzai A.W., Susskind M.M., Sauer R.T. SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J. 18:1999;3793-3799.
    • (1999) EMBO J. , vol.18 , pp. 3793-3799
    • Karzai, A.W.1    Susskind, M.M.2    Sauer, R.T.3
  • 8
    • 0034646235 scopus 로고    scopus 로고
    • Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli
    • Barends S., Wower J., Kraal B. Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli. Biochemistry. 39:2000;2652-2658.
    • (2000) Biochemistry , vol.39 , pp. 2652-2658
    • Barends, S.1    Wower, J.2    Kraal, B.3
  • 9
    • 0032840381 scopus 로고    scopus 로고
    • Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu
    • Rudinger-Thirion J., Giege R., Felden B. Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu. RNA. 5:1999;989-992.
    • (1999) RNA , vol.5 , pp. 989-992
    • Rudinger-Thirion, J.1    Giege, R.2    Felden, B.3
  • 10
    • 0034423519 scopus 로고    scopus 로고
    • Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome
    • Wower I.K., Zwieb C.W., Guven S.A., Wower J. Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome. EMBO J. 19:2000;6612-6621.
    • (2000) EMBO J. , vol.19 , pp. 6612-6621
    • Wower, I.K.1    Zwieb, C.W.2    Guven, S.A.3    Wower, J.4
  • 11
    • 0028170454 scopus 로고
    • TRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis
    • Ushida C., Himeno H., Watanabe T., Muto A. tRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis. Nucl. Acids Res. 22:1994;3392-3396.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3392-3396
    • Ushida, C.1    Himeno, H.2    Watanabe, T.3    Muto, A.4
  • 13
    • 0035171382 scopus 로고    scopus 로고
    • Emerging views on tmRNA-mediated protein tagging and ribosome rescue
    • Gillet R., Felden B. Emerging views on tmRNA-mediated protein tagging and ribosome rescue. Mol. Microbiol. 42:2001;879-885.
    • (2001) Mol. Microbiol. , vol.42 , pp. 879-885
    • Gillet, R.1    Felden, B.2
  • 14
    • 0034046020 scopus 로고    scopus 로고
    • The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue
    • Karzai A.W., Roche E.D., Sauer R.T. The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue. Nature Struct. Biol. 7:2000;449-455.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 15
    • 0028906813 scopus 로고
    • C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide
    • Tu G.F., Reid G.E., Zhang J.G., Moritz R.L., Simpson R.J. C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide. J. Biol. Chem. 270:1995;9322-9326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9322-9326
    • Tu, G.F.1    Reid, G.E.2    Zhang, J.G.3    Moritz, R.L.4    Simpson, R.J.5
  • 16
    • 0029987860 scopus 로고    scopus 로고
    • 10Sa RNA is associated with 70 S ribosome particles in Escherichia coli
    • Komine Y., Kitabatake M., Inokuchi H. 10Sa RNA is associated with 70 S ribosome particles in Escherichia coli. J. Biochem. (Tokyo). 119:1996;463-467.
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 463-467
    • Komine, Y.1    Kitabatake, M.2    Inokuchi, H.3
  • 17
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. The structural basis of ribosome activity in peptide bond synthesis. Science. 289:2000;920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 18
    • 0030020935 scopus 로고    scopus 로고
    • When proteins receive deadly messages at birth
    • Jentsch S. When proteins receive deadly messages at birth. Science. 271:1996;955-956.
    • (1996) Science , vol.271 , pp. 955-956
    • Jentsch, S.1
  • 20
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S., Roche E., Zhou Y., Sauer R.T. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1998;1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 21
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman C., Thevenet D., Bouloc P., Walker G.C., D'Ari R. Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12:1998;1348-1355.
    • (1998) Genes Dev. , vol.12 , pp. 1348-1355
    • Herman, C.1    Thevenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 22
    • 0033575660 scopus 로고    scopus 로고
    • SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity
    • Roche E.D., Sauer R.T. SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity. EMBO J. 18:1999;4579-4589.
    • (1999) EMBO J. , vol.18 , pp. 4579-4589
    • Roche, E.D.1    Sauer, R.T.2
  • 23
    • 0036850399 scopus 로고    scopus 로고
    • The C-terminal amino acid sequence of nascent peptide is a major determinant of SsrA tagging at all three stop codons
    • Sunohara T., Abo T., Inada T., Aiba H. The C-terminal amino acid sequence of nascent peptide is a major determinant of SsrA tagging at all three stop codons. RNA. 8:2002;1416-1427.
    • (2002) RNA , vol.8 , pp. 1416-1427
    • Sunohara, T.1    Abo, T.2    Inada, T.3    Aiba, H.4
  • 24
    • 0036364355 scopus 로고    scopus 로고
    • Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli
    • Collier J., Binet E., Bouloc P. Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli. Mol. Microbiol. 45:2002;745-754.
    • (2002) Mol. Microbiol. , vol.45 , pp. 745-754
    • Collier, J.1    Binet, E.2    Bouloc, P.3
  • 25
    • 0035958905 scopus 로고    scopus 로고
    • Identification of endogenous SsrA-tagged proteins reveals tagging at positions corresponding to stop codons
    • Roche E.D., Sauer R.T. Identification of endogenous SsrA-tagged proteins reveals tagging at positions corresponding to stop codons. J. Biol. Chem. 276:2001;28509-28515.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28509-28515
    • Roche, E.D.1    Sauer, R.T.2
  • 26
    • 0242361562 scopus 로고    scopus 로고
    • Cleavage of the a site mRNA codon during ribosome pausing provides a mechanism for translational quality control
    • Hayes C.S., Sauer R.T. Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Mol. Cell. 12:2003;903-911.
    • (2003) Mol. Cell , vol.12 , pp. 903-911
    • Hayes, C.S.1    Sauer, R.T.2
  • 28
    • 0035958587 scopus 로고    scopus 로고
    • The path of messenger RNA through the ribosome
    • Yusupova G.Z., Yusupov M.M., Cate J.H., Noller H.F. The path of messenger RNA through the ribosome. Cell. 106:2001;233-241.
    • (2001) Cell , vol.106 , pp. 233-241
    • Yusupova, G.Z.1    Yusupov, M.M.2    Cate, J.H.3    Noller, H.F.4
  • 29
    • 1842596222 scopus 로고    scopus 로고
    • Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli
    • In the press
    • In the press Sunohara T., Jojima K., Tagami H., Inada T., Aiba H. Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli. J. Biol. Chem. 2004.
    • (2004) J. Biol. Chem.
    • Sunohara, T.1    Jojima, K.2    Tagami, H.3    Inada, T.4    Aiba, H.5
  • 30
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • Christensen S.K., Gerdes K. RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol. Microbiol. 48:2003;1389-1400.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 31
    • 0018498843 scopus 로고
    • Nucleoside triphosphate regeneration decreases the frequency of translation errors
    • Jelenc P.C., Kurland C.G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci. USA. 76:1979;3174-3178.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 3174-3178
    • Jelenc, P.C.1    Kurland, C.G.2
  • 32
    • 0027991544 scopus 로고
    • In vitro transcription: Preparative RNA yields in analytical scale reactions
    • Pokrovskaya I.D., Gurevich V.V. In vitro transcription: preparative RNA yields in analytical scale reactions. Anal. Biochem. 220:1994;420-423.
    • (1994) Anal. Biochem. , vol.220 , pp. 420-423
    • Pokrovskaya, I.D.1    Gurevich, V.V.2
  • 33
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer D.V., Pavlov M.Y., MacDougall J., Buckingham R.H., Ehrenberg M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 16:1997;4126-4133.
    • (1997) EMBO J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 34
    • 0030779476 scopus 로고    scopus 로고
    • Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site
    • Pavlov M.Y., Freistroffer D.V., Heurgue-Hamard V., Buckingham R.H., Ehrenberg M. Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site. J. Mol. Biol. 273:1997;389-401.
    • (1997) J. Mol. Biol. , vol.273 , pp. 389-401
    • Pavlov, M.Y.1    Freistroffer, D.V.2    Heurgue-Hamard, V.3    Buckingham, R.H.4    Ehrenberg, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.