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Volumn 16, Issue 5, 2010, Pages 980-990

Role of the C-terminal tail of SmpB in the early stage of trans-translation

Author keywords

Ribosome; SmpB; TmRNA; Trans translation; Translation

Indexed keywords

ALANINE TRANSFER RNA; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE; HYDROXYL RADICAL; MESSENGER RNA; PEPTIDYLTRANSFERASE; PROTEIN; SMPB PROTEIN; SYNTHETIC PEPTIDE; TRANSFER RNA; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 77951184072     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1916610     Document Type: Article
Times cited : (29)

References (54)
  • 2
    • 0343627965 scopus 로고    scopus 로고
    • SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon
    • Abo T, Inada T, Ogawa K, Aiba H. 2000. SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon. EMBO J 19: 3762-3769.
    • (2000) EMBO J , vol.19 , pp. 3762-3769
    • Abo, T.1    Inada, T.2    Ogawa, K.3    Aiba, H.4
  • 3
    • 26944432029 scopus 로고    scopus 로고
    • Competition between trans-translation and termination or elongation of translation
    • Asano K, Kurita D, Takada K, Konno T, Muto A, Himeno H. 2005. Competition between trans-translation and termination or elongation of translation. Nucleic Acids Res 33: 5544-5552.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5544-5552
    • Asano, K.1    Kurita, D.2    Takada, K.3    Konno, T.4    Muto, A.5    Himeno, H.6
  • 4
    • 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. 2000. Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli. Biochemistry 39: 2652-2658.
    • (2000) Biochemistry , vol.39 , pp. 2652-2658
    • Barends, S.1    Wower, J.2    Kraal, B.3
  • 5
    • 0035900548 scopus 로고    scopus 로고
    • Simultaneous and functional binding of SmpB and EF-Tu-TP to the alanyl acceptor arm of tmRNA
    • Barends S, Karzai AW, Sauer RT, Wower J, Kraal B. 2001. Simultaneous and functional binding of SmpB and EF-Tu-TP to the alanyl acceptor arm of tmRNA. J Mol Biol 314: 9-21.
    • (2001) J Mol Biol , vol.314 , pp. 9-21
    • Barends, S.1    Karzai, A.W.2    Sauer, R.T.3    Wower, J.4    Kraal, B.5
  • 7
    • 0037007224 scopus 로고    scopus 로고
    • Structure of small protein B: The protein component of the tmRNA-SmpB system for ribosome rescue
    • Dong G, Nowakowski J, Hoffman DW. 2002. Structure of small protein B: The protein component of the tmRNA-SmpB system for ribosome rescue. EMBO J 21: 1845-1854.
    • (2002) EMBO J , vol.21 , pp. 1845-1854
    • Dong, G.1    Nowakowski, J.2    Hoffman, D.W.3
  • 8
    • 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 JF, Himeno H, Muto A, Gesteland RF, McCloskey JA, Crain PF. 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
  • 10
    • 34250380391 scopus 로고    scopus 로고
    • Scaffolding as an organizing principle in trans-translation. the roles of small protein B and ribosomal protein S1
    • Gillet R, Kaur S, Li W, Hallier M, Felden B, Frank J. 2006. Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1. J Biol Chem 282: 6356-6363.
    • (2006) J Biol Chem , vol.282 , pp. 6356-6363
    • Gillet, R.1    Kaur, S.2    Li, W.3    Hallier, M.4    Felden, B.5    Frank, J.6
  • 11
    • 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 RT. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes & Dev 12: 1338-1347.
    • (1998) Genes & Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 12
    • 0041737720 scopus 로고    scopus 로고
    • Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB
    • Gutmann S, Haebel PW, Metzinger L, Sutter M, Felden B, Ban N. 2003. Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB. Nature 424: 699-703.
    • (2003) Nature , vol.424 , pp. 699-703
    • Gutmann, S.1    Haebel, P.W.2    Metzinger, L.3    Sutter, M.4    Felden, B.5    Ban, N.6
  • 13
    • 33645802168 scopus 로고    scopus 로고
    • Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation
    • Hallier M, Desreac J, Felden B. 2006. Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation. Nucleic Acids Res 34: 1935-1943.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1935-1943
    • Hallier, M.1    Desreac, J.2    Felden, B.3
  • 14
    • 0035890475 scopus 로고    scopus 로고
    • Importance of the conserved nucleotides around the tRNA-like structure of Escherichia coli transfer-messenger RNA for protein tagging
    • Hanawa-Suetsugu K, Bordeau V, Himeno H, Muto A, Felden B. 2001. Importance of the conserved nucleotides around the tRNA-like structure of Escherichia coli transfer-messenger RNA for protein tagging. Nucleic Acids Res 29: 4663-4673.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4663-4673
    • Hanawa-Suetsugu, K.1    Bordeau, V.2    Himeno, H.3    Muto, A.4    Felden, B.5
  • 18
    • 77951202828 scopus 로고    scopus 로고
    • Trans-translation by tmRNA and a protein mimicking tRNA and mRNA
    • eds. TE Esterhouse and LB Petrinos, Nova Science Publishers Inc., New York
    • Himeno H, Kurita D, Muto A. 2009. Trans-translation by tmRNA and a protein mimicking tRNA and mRNA. In Protein biosynthesis (eds. TE Esterhouse and LB Petrinos), pp. 69-107. Nova Science Publishers Inc., New York.
    • (2009) Protein Biosynthesis , pp. 69-107
    • Himeno, H.1    Kurita, D.2    Muto, A.3
  • 19
    • 22144462503 scopus 로고    scopus 로고
    • Cell cycle-regulated degradation of tmRNA is controlled by RNase R and SmpB
    • Hong SJ, Tran QA, Keiler KC. 2005. Cell cycle-regulated degradation of tmRNA is controlled by RNase R and SmpB. Mol Microbiol 57: 565-575.
    • (2005) Mol Microbiol , vol.57 , pp. 565-575
    • Hong, S.J.1    Tran, Q.A.2    Keiler, K.C.3
  • 20
    • 0034161440 scopus 로고    scopus 로고
    • Charged tmRNA but not tmRNA-mediated proteolysis is essential for Neisseria gonorrhoeae viability
    • Huang C, Wolfgang MC, Withey J, Koomey M, Friedman DI. 2000. Charged tmRNA but not tmRNA-mediated proteolysis is essential for Neisseria gonorrhoeae viability. EMBO J 19: 1098-1107.
    • (2000) EMBO J , vol.19 , pp. 1098-1107
    • Huang, C.1    Wolfgang, M.C.2    Withey, J.3    Koomey, M.4    Friedman, D.I.5
  • 22
    • 14044265657 scopus 로고    scopus 로고
    • Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form
    • Jacob Y, Sharkady SM, Bhardwaj K, Sanda A, Williams KP. 2005. Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form. J Biol Chem 280: 5503-5509.
    • (2005) J Biol Chem , vol.280 , pp. 5503-5509
    • Jacob, Y.1    Sharkady, S.M.2    Bhardwaj, K.3    Sanda, A.4    Kp, W.5
  • 23
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • Karzai AW, Susskind MM, Sauer RT. 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
  • 24
    • 33750838456 scopus 로고    scopus 로고
    • Cryo-EM visualization of transfer messenger RNA with two SmpBs in a stalled ribosome
    • Kaur S, Gillet R, Li W, Gursky R, Frank J. 2006. Cryo-EM visualization of transfer messenger RNA with two SmpBs in a stalled ribosome. Proc Natl Acad Sci 103: 16484-16489.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 16484-16489
    • Kaur, S.1    Gillet, R.2    Li, W.3    Gursky, R.4    Frank, J.5
  • 25
    • 34247165146 scopus 로고    scopus 로고
    • Physiology of tmRNA: What gets tagged and why?
    • Keiler KC. 2007. Physiology of tmRNA: What gets tagged and why? Curr Opin Microbiol 10: 169-175.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 169-175
    • Keiler, K.C.1
  • 26
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC, Waller PR, Sauer RT. 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
  • 27
    • 0028124122 scopus 로고
    • A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli
    • Komine Y, Kitabatake M, Yokogawa T, Nishikawa K, Inokuchi H. 1994. A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli. Proc Natl Acad Sci 91: 9223-9227.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 9223-9227
    • Komine, Y.1    Kitabatake, M.2    Yokogawa, T.3    Nishikawa, K.4    Inokuchi, H.5
  • 28
    • 34748881977 scopus 로고    scopus 로고
    • A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation
    • Konno T, Kurita D, Takada K, Muto A, Himeno H. 2007. A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation. RNA 13: 1723-1731.
    • (2007) RNA , vol.13 , pp. 1723-1731
    • Konno, T.1    Kurita, D.2    Takada, K.3    Muto, A.4    Himeno, H.5
  • 29
    • 37549063937 scopus 로고    scopus 로고
    • Interaction of SmpB with ribosome from directed hydroxyl radical probing
    • Kurita D, Sasaki R, Muto A, Himeno H. 2007. Interaction of SmpB with ribosome from directed hydroxyl radical probing. Nucleic Acids Res 35: 7248-7255.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7248-7255
    • Kurita, D.1    Sasaki, R.2    Muto, A.3    Himeno, H.4
  • 30
    • 0032540286 scopus 로고    scopus 로고
    • NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif
    • Legault P, Li J, Mogridge J, Kay LE, Greenblatt J. 1998. NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif. Cell 93: 289-299.
    • (1998) Cell , vol.93 , pp. 289-299
    • Legault, P.1    Li, J.2    Mogridge, J.3    Kay, L.E.4    Greenblatt, J.5
  • 31
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • Moore SD, Sauer RT. 2007. The tmRNA system for translational surveillance and ribosome rescue. Annu Rev Biochem 76: 101 124.
    • (2007) Annu Rev Biochem , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 32
    • 0031939779 scopus 로고    scopus 로고
    • A bacterial RNA that functions as both a tRNA and an mRNA
    • Muto A, Ushida C, 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
  • 33
    • 0033873650 scopus 로고    scopus 로고
    • Requirement of transfer-messenger RNA for the growth of Bacillus subtilis under stresses
    • Muto A, Fujihara A, Ito K, Matsuno J, Ushida C, Himeno H. 2000. Requirement of transfer-messenger RNA for the growth of Bacillus subtilis under stresses. Genes Cells 5: 627-635.
    • (2000) Genes Cells , vol.5 , pp. 627-635
    • Muto, A.1    Fujihara, A.2    Ito, K.3    Matsuno, J.4    Ushida, C.5    Himeno, H.6
  • 34
    • 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 JF, Gesteland RF, Himeno H, Muto A. 1999. 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
  • 37
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle JM, Ramakrishnan V. 2005. Structural insights into translational fidelity. Annu Rev Biochem 74: 129-177.
    • (2005) Annu Rev Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 38
    • 34047097775 scopus 로고    scopus 로고
    • Ribosomal protein S1 is not essential for the trans-translation machinery
    • Qi H, Shimizu Y, Ueda T. 2007. Ribosomal protein S1 is not essential for the trans-translation machinery. J Mol Biol 368: 845-852.
    • (2007) J Mol Biol , vol.368 , pp. 845-852
    • Qi, H.1    Shimizu, Y.2    Ueda, T.3
  • 39
    • 0034923932 scopus 로고    scopus 로고
    • Fidelity of aminoacyl-tRNA selection on the ribosome: Kinetic and structural mechanisms
    • Rodnina MV, Wintermeyer W. 2001. Fidelity of aminoacyl-tRNA selection on the ribosome: Kinetic and structural mechanisms. Annu Rev Biochem 70: 415-435.
    • (2001) Annu Rev Biochem , vol.70 , pp. 415-435
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 40
    • 0032840381 scopus 로고    scopus 로고
    • Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu
    • Rudinger-Thirion J, Giegé R, Felden B. 1999. Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu. RNA 5: 989-992.
    • (1999) RNA , vol.5 , pp. 989-992
    • Rudinger-Thirion, J.1    Giegé, R.2    Felden, B.3
  • 42
    • 0000641399 scopus 로고    scopus 로고
    • Antitermination in bacteriophage l. the structure of the N36 peptide-boxB RNA complex
    • Scharpf M, Sticht H, Schweimer K, Boehm M, Hoffmann S, Rosch P. 2000. Antitermination in bacteriophage l. The structure of the N36 peptide-boxB RNA complex. Eur J Biochem 267: 2397-2408.
    • (2000) Eur J Biochem , vol.267 , pp. 2397-2408
    • Scharpf, M.1    Sticht, H.2    Schweimer, K.3    Boehm, M.4    Hoffmann, S.5    Rosch, P.6
  • 43
    • 0037029092 scopus 로고    scopus 로고
    • The role of SmpB protein in trans-translation
    • Shimizu Y, Ueda T. 2002. The role of SmpB protein in trans-translation. FEBS Lett 514: 74-77.
    • (2002) FEBS Lett , vol.514 , pp. 74-77
    • Shimizu, Y.1    Ueda, T.2
  • 44
    • 33744947098 scopus 로고    scopus 로고
    • SmpB triggers GTP hydrolysis of elongation factor Tu on ribosomes by compensating for the lack of codon-anticodon interaction during trans-translation initiation
    • Shimizu Y, Ueda T. 2006. SmpB triggers GTP hydrolysis of elongation factor Tu on ribosomes by compensating for the lack of codon-anticodon interaction during trans-translation initiation. J Biol Chem 281: 15987-15996.
    • (2006) J Biol Chem , vol.281 , pp. 15987-15996
    • Shimizu, Y.1    Ueda, T.2
  • 46
    • 0037313461 scopus 로고    scopus 로고
    • TmRNA from Thermus thermophilus. Interaction with alanyl-tRNA synthetase and elongation factor Tu
    • Stepanov VG, Nyborg J. 2003. tmRNA from Thermus thermophilus. Interaction with alanyl-tRNA synthetase and elongation factor Tu. Eur J Biochem 270: 463-475.
    • (2003) Eur J Biochem , vol.270 , pp. 463-475
    • Stepanov, V.G.1    Nyborg, J.2
  • 47
    • 36849093840 scopus 로고    scopus 로고
    • Functional SmpB-ribosome interactions require tmRNA
    • Sundermeier TR, Karzai AW. 2007. Functional SmpB-ribosome interactions require tmRNA. J Biol Chem 282: 34779-34786.
    • (2007) J Biol Chem , vol.282 , pp. 34779-34786
    • Sundermeier, T.R.1    Karzai, A.W.2
  • 48
    • 14044271596 scopus 로고    scopus 로고
    • A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans-translation
    • Sundermeier TR, Dulebohn DP, Cho HJ, Karzai AW. 2005. A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans-translation. Proc Natl Acad Sci 102: 2316-2321.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 2316-2321
    • Sundermeier, T.R.1    Dulebohn, D.P.2    Cho, H.J.3    Karzai, A.W.4
  • 50
    • 0028170454 scopus 로고
    • TRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis
    • Ushida C, Himeno H, Watanabe T, 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
  • 52
    • 0034423519 scopus 로고    scopus 로고
    • Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome
    • Wower IK, Zwieb CW, Guven SA, Wower J. 2000. Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome. EMBO J 19: 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
  • 53
    • 0037118708 scopus 로고    scopus 로고
    • SmpB: A protein that binds to double-stranded segments in tmRNA and tRNA
    • Wower J, Zwieb CW, Hoffman DW, Wower IK. 2002. SmpB: A protein that binds to double-stranded segments in tmRNA and tRNA. Biochemistry 41: 8826-8836.
    • (2002) Biochemistry , vol.41 , pp. 8826-8836
    • Wower, J.1    Zwieb, C.W.2    Hoffman, D.W.3    Wower, I.K.4
  • 54
    • 33751103912 scopus 로고    scopus 로고
    • Structural basis for messenger RNA movement on the ribosome
    • Yusupova G, Jenner L, Rees B, Moras D, Yusupov M. 2006. Structural basis for messenger RNA movement on the ribosome. Nature 444: 391-394.
    • (2006) Nature , vol.444 , pp. 391-394
    • Yusupova, G.1    Jenner, L.2    Rees, B.3    Moras, D.4    Yusupov, M.5


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