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Volumn 18, Issue 19, 1999, Pages 5423-5433

Resuming translation on tmRNA: A unique mode of determining a reading frame

Author keywords

10Sa RNA; Protein degradation; Reading frame; Ribosome; Translational initiation

Indexed keywords

ADENOSINE; MESSENGER RNA;

EID: 0033215307     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.19.5423     Document Type: Article
Times cited : (91)

References (32)
  • 1
    • 0001755271 scopus 로고    scopus 로고
    • Dynamics of the genetic code
    • Gesteland, R.F., Cech, T.R. and Atkins, J.F. (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Atkins, J.F., Böck, A., Matsufuji, S. and Gesteland, R.F. (1999) Dynamics of the genetic code. In Gesteland, R.F., Cech, T.R. and Atkins, J.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 637-673.
    • (1999) The RNA World , pp. 637-673
    • Atkins, J.F.1    Böck, A.2    Matsufuji, S.3    Gesteland, R.F.4
  • 2
    • 0029670766 scopus 로고    scopus 로고
    • Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA and a truncated R1pA
    • Bass, S., Gu, Q. and Christen, A. (1996) Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA and a truncated R1pA. J. Bacteriol., 178, 1154-1161.
    • (1996) J. Bacteriol. , vol.178 , pp. 1154-1161
    • Bass, S.1    Gu, Q.2    Christen, A.3
  • 3
    • 0032212454 scopus 로고    scopus 로고
    • Analysis of recombinant human ADP-ribosylation factors by reversed-phase high-performance liquid chromatography and electrospray mass spectrometry
    • Berger, S.J., Claude, A.C. and Melançon, P. (1998) Analysis of recombinant human ADP-ribosylation factors by reversed-phase high-performance liquid chromatography and electrospray mass spectrometry. Anal. Biochem., 264, 53-65.
    • (1998) Anal. Biochem. , vol.264 , pp. 53-65
    • Berger, S.J.1    Claude, A.C.2    Melançon, P.3
  • 4
    • 0017655183 scopus 로고
    • The attenuator of the tryptophan operon of Escherichia coli. Heterogeneous 3′-OH termini in vivo and deletion mapping of functions
    • Bertrand, K., Korn, L.J., Lee, F. and Yanofsky, C. (1977) The attenuator of the tryptophan operon of Escherichia coli. Heterogeneous 3′-OH termini in vivo and deletion mapping of functions. J. Mol. Biol., 117, 227-247.
    • (1977) J. Mol. Biol. , vol.117 , pp. 227-247
    • Bertrand, K.1    Korn, L.J.2    Lee, F.3    Yanofsky, C.4
  • 5
    • 0030457112 scopus 로고    scopus 로고
    • Programmed translational frameshifting
    • Farabaugh, P.J. (1996) Programmed translational frameshifting. Annu. Rev. Genet., 30, 507-528.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 507-528
    • Farabaugh, P.J.1
  • 7
    • 0032101712 scopus 로고    scopus 로고
    • Presence and location of modified nucleotides in Escherichia coli tmRNA: Structural mimicry with tRNA acceptor branches
    • Felden, B., Hanawa, K., Atkins, J.F., Himeno, H., Muto, A., Gesteland, R.F., McCloskey, J.A. and Crain, P.F. (1998) Presence and location of modified nucleotides in Escherichia coli tmRNA: structural mimicry with tRNA acceptor branches. EMBO J., 17, 3188-3196.
    • (1998) EMBO J. , vol.17 , pp. 3188-3196
    • Felden, B.1    Hanawa, K.2    Atkins, J.F.3    Himeno, H.4    Muto, A.5    Gesteland, R.F.6    McCloskey, J.A.7    Crain, P.F.8
  • 8
    • 0029896020 scopus 로고    scopus 로고
    • Receding: Dynamic reprogramming of translation
    • Gesteland, R.F. and Atkins, J.F. (1996) Receding: dynamic reprogramming of translation. Annu. Rev. Biochem., 65, 741-768.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 741-768
    • Gesteland, R.F.1    Atkins, J.F.2
  • 9
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz, D., McPheeters, D.S., Traut, R. and Gold, L. (1988) Extension inhibition analysis of translation initiation complexes. Methods Enzymol., 164, 419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4
  • 10
    • 0032511223 scopus 로고    scopus 로고
    • A nickel complex cleaves uridine in folded RNA structures: Application to E.coli tmRNA and related engineered molecules
    • Hickerson, R.P., Watkins-Sims, C.D., Burrows, C.J., Atkins, J.F., Gesteland, R.F. and Felden, B. (1998) A nickel complex cleaves uridine in folded RNA structures: application to E.coli tmRNA and related engineered molecules. J. Mol. Biol., 279, 577-587.
    • (1998) J. Mol. Biol. , vol.279 , pp. 577-587
    • Hickerson, R.P.1    Watkins-Sims, C.D.2    Burrows, C.J.3    Atkins, J.F.4    Gesteland, R.F.5    Felden, B.6
  • 11
  • 12
    • 0023909946 scopus 로고
    • A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60
    • Huang, W.M., Ao, S.Z., Casjens, S., Orlandi, R., Zeikus, R., Weiss, R., Winge, D. and Fang, M. (1988) A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60. Science, 239, 1005-1012.
    • (1988) Science , vol.239 , pp. 1005-1012
    • Huang, W.M.1    Ao, S.Z.2    Casjens, S.3    Orlandi, R.4    Zeikus, R.5    Weiss, R.6    Winge, D.7    Fang, M.8
  • 13
    • 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. and Sauer, R.T. (1999) SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J., 18, 3793-3799.
    • (1999) EMBO J. , vol.18 , pp. 3793-3799
    • Karzai, A.W.1    Susskind, M.M.2    Sauer, R.T.3
  • 14
    • 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. and Sauer, R.T. (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science, 271, 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 15
    • 0029843213 scopus 로고    scopus 로고
    • The DegP and DegQ periplasmic endoproteases of Escherichia coli: Specificity for cleavage sites and substrate conformation
    • Kolmar, H., Waller, P.R. and Sauer, R.T. (1996) The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation. J. Bacteriol., 178, 5925-5929.
    • (1996) J. Bacteriol. , vol.178 , pp. 5925-5929
    • Kolmar, H.1    Waller, P.R.2    Sauer, R.T.3
  • 16
  • 17
    • 0031939779 scopus 로고    scopus 로고
    • A bacterial RNA that functions as both a tRNA and an mRNA
    • Muto, A., Ushida, C. and Himeno, H. (1998) A bacterial RNA that functions as both a tRNA and an mRNA. Trends Biochem. Sci., 23, 25-29.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 25-29
    • Muto, A.1    Ushida, C.2    Himeno, H.3
  • 18
    • 0033605218 scopus 로고    scopus 로고
    • Functional and structural analysis of a pseudoknot upstream of the tag-encoded sequence in E.coli tmRNA
    • Nameki, N., Felden, B., Atkins, J.F., Gesteland, R.F., Himeno, H. and Muto, A. (1999a) Functional and structural analysis of a pseudoknot upstream of the tag-encoded sequence in E.coli tmRNA. J. Mol. Biol., 286, 733-744.
    • (1999) J. Mol. Biol. , vol.286 , pp. 733-744
    • Nameki, N.1    Felden, B.2    Atkins, J.F.3    Gesteland, R.F.4    Himeno, H.5    Muto, A.6
  • 19
    • 0033612218 scopus 로고    scopus 로고
    • Amino acid acceptor identity switch of Escherichia coli tmRNA from alanine to histidine in vitro
    • Nameki, N., Tadaki, T., Muto, A. and Himeno, H. (1999b) Amino acid acceptor identity switch of Escherichia coli tmRNA from alanine to histidine in vitro. J. Mol. Biol., 289, 1-7.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1-7
    • Nameki, N.1    Tadaki, T.2    Muto, A.3    Himeno, H.4
  • 20
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • Powers, T. and Waller, P. (1997) Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J., 16, 4880-4886.
    • (1997) EMBO J. , vol.16 , pp. 4880-4886
    • Powers, T.1    Waller, P.2
  • 21
    • 0033575660 scopus 로고    scopus 로고
    • SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity
    • Roche, E.D. and Sauer, R.T. (1999) SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity. EMBO J., 18, 4579-4589.
    • (1999) EMBO J. , vol.18 , pp. 4579-4589
    • Roche, E.D.1    Sauer, R.T.2
  • 22
    • 0022896751 scopus 로고
    • Mapping and complementation studies of the gene for release factor 1
    • Ryden, M., Murphy, J., Martin, R., Isaksson, L. and Gallant, J. (1986) Mapping and complementation studies of the gene for release factor 1. J. Bacteriol., 168, 1066-1069.
    • (1986) J. Bacteriol. , vol.168 , pp. 1066-1069
    • Ryden, M.1    Murphy, J.2    Martin, R.3    Isaksson, L.4    Gallant, J.5
  • 23
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T.D. and Stephens, R.M. (1990) Sequence logos: a new way to display consensus sequences. Nucleic Acids Res., 18, 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 24
    • 0028084846 scopus 로고
    • Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12
    • Silber, K.R. and Sauer, R.T. (1994) Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12. Mol. Gen. Genet., 242, 237-240.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 237-240
    • Silber, K.R.1    Sauer, R.T.2
  • 25
    • 0007981475 scopus 로고
    • Ribosome recognition of initiator regions in the RNA bacteriophage genome
    • Zinder, N. (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Steitz, J.A. (1975) Ribosome recognition of initiator regions in the RNA bacteriophage genome. In Zinder, N. (ed.), RNA Phages. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 319-352.
    • (1975) RNA Phages , pp. 319-352
    • Steitz, J.A.1
  • 26
    • 0029773416 scopus 로고    scopus 로고
    • Three, four or more: The translational stop signal at length
    • Tate, W.P. and Mannering, S.A. (1996) Three, four or more: the translational stop signal at length. Mol. Microbiol., 21, 213-219.
    • (1996) Mol. Microbiol. , vol.21 , pp. 213-219
    • Tate, W.P.1    Mannering, S.A.2
  • 27
    • 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. and Simpson, R.J. (1995) C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide. J. Biol. Chem., 270, 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
  • 28
    • 0028170454 scopus 로고
    • tRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis
    • Ushida, C., Himeno, H., Watanabe, T. and Muto, A. (1994) tRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis. Nucleic Acids Res., 22, 3392-3396.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3392-3396
    • Ushida, C.1    Himeno, H.2    Watanabe, T.3    Muto, A.4
  • 29
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • Waller, P.R. and Sauer, R.T. (1996) Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol., 178, 1146-1153.
    • (1996) J. Bacteriol. , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 30
    • 0025312745 scopus 로고
    • A nascent peptide is required for ribosomal bypass of the coding gap in bacteriophage T4 gene 60
    • Weiss, R.B., Huang, W.M. and Dunn, D.M. (1990) A nascent peptide is required for ribosomal bypass of the coding gap in bacteriophage T4 gene 60. Cell, 62, 117-126.
    • (1990) Cell , vol.62 , pp. 117-126
    • Weiss, R.B.1    Huang, W.M.2    Dunn, D.M.3
  • 31
    • 0032919367 scopus 로고    scopus 로고
    • The tmRNA website
    • Williams, K.P. (1999) The tmRNA website. Nucleic Acids Res., 27, 165-166.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 165-166
    • Williams, K.P.1
  • 32
    • 0029907105 scopus 로고    scopus 로고
    • Phylogenetic analysis of tmRNA secondary structure
    • Williams, K.P. and Bartel, D.P. (1996) Phylogenetic analysis of tmRNA secondary structure. RNA, 2, 1306-1310.
    • (1996) RNA , vol.2 , pp. 1306-1310
    • Williams, K.P.1    Bartel, D.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.