메뉴 건너뛰기




Volumn , Issue , 2009, Pages 69-108

Trans-translation by tmRNA and a protein mimicking tRNA and mRNA

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77951202828     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (198)
  • 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. (2002). SsrA-mediated protein tagging in the presence of miscoding drugs and its physiological role in Escherichia coli. Genes Cells, 7, 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
  • 3
    • 0037154255 scopus 로고    scopus 로고
    • A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae
    • Akerley, B.J., Rubin, E.J., Novick, V.L., Amaya, K., Judson, N., & Mekalanos, J.J. (2002). A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae. Proc. Natl. Acad. Sci. USA, 99, 966-971.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 966-971
    • Akerley, B.J.1    Rubin, E.J.2    Novick, V.L.3    Amaya, K.4    Judson, N.5    Mekalanos, J.J.6
  • 5
    • 0029824009 scopus 로고    scopus 로고
    • 10Sa RNA complements the temperature-sensitive phenotype caused by a mutation in the phosphoribosyl pyrophosphate synthetase (prs) gene in Escherichia coli
    • Ando, H., Kitabatake, M., & Inokuchi, H. (1996). 10Sa RNA complements the temperature-sensitive phenotype caused by a mutation in the phosphoribosyl pyrophosphate synthetase (prs) gene in Escherichia coli. Genes Genet. Syst., 71, 47-50.
    • (1996) Genes Genet. Syst , vol.71 , pp. 47-50
    • Ando, H.1    Kitabatake, M.2    Inokuchi, H.3
  • 6
    • 0027223104 scopus 로고
    • Recognition nucleotides of Escherichia coli tRNALeu and its elements facilitating discrimination from tRNASer and tRNATyr
    • Asahara, H., Himeno, H., Tamura, K., Hasegawa, T., Watanabe, K., & Shimizu, M. (1993). Recognition nucleotides of Escherichia coli tRNALeu and its elements facilitating discrimination from tRNASer and tRNATyr. J. Mol. Biol., 231, 219-229.
    • (1993) J. Mol. Biol , vol.231 , pp. 219-229
    • Asahara, H.1    Himeno, H.2    Tamura, K.3    Hasegawa, T.4    Watanabe, K.5    Shimizu, M.6
  • 7
    • 0028268618 scopus 로고
    • Escherichia coli seryl-tRNA synthetase recognizes tRNASer by its characteristic tertiary structure
    • Asahara, H., Himeno, H., Tamura, K., Nameki, N., Hasegawa, T., & Shimizu, M. (1994). Escherichia coli seryl-tRNA synthetase recognizes tRNASer by its characteristic tertiary structure. J. Mol. Biol., 236, 738-748.
    • (1994) J. Mol. Biol , vol.236 , pp. 738-748
    • Asahara, H.1    Himeno, H.2    Tamura, K.3    Nameki, N.4    Hasegawa, T.5    Shimizu, M.6
  • 8
    • 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
  • 9
    • 0030026177 scopus 로고    scopus 로고
    • A case for trans translation
    • Atkins, J. F., & Gesteland, R. F. (1996). A case for trans translation. Nature, 379, 769-770.
    • (1996) Nature , vol.379 , pp. 769-770
    • Atkins, J.F.1    Gesteland, R.F.2
  • 10
    • 34447331273 scopus 로고    scopus 로고
    • Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits
    • Barat, C., Datta, P.P., Raj, V.S., Sharma, M.R., Kaji, H., Kaji, A., & Agrawal, R.K. (2007). Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits. Mol. Cell, 27, 250-261.
    • (2007) Mol. Cell , vol.27 , pp. 250-261
    • Barat, C.1    Datta, P.P.2    Raj, V.S.3    Sharma, M.R.4    Kaji, H.5    Kaji, A.6    Agrawal, R.K.7
  • 11
    • 0028215784 scopus 로고
    • Salmonella typhimurium loci involved in survival within macrophages
    • Bäumler, A.J., Kusters, J.G., Stojiljkovic, I., & Heffron, F. (1994). Salmonella typhimurium loci involved in survival within macrophages. Infect. Immun., 62, 1632-1630.
    • (1994) Infect. Immun , vol.62 , pp. 1632-1630
    • Bäumler, A.J.1    Kusters, J.G.2    Stojiljkovic, I.3    Heffron, F.4
  • 12
    • 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
  • 13
    • 0035900548 scopus 로고    scopus 로고
    • Simultaneous and functional binding of SmpB and EF-Tu-GTP to the alanyl acceptor arm of tmRNA
    • Barends, S., Karzai, A. W., Sauer, R. T., Wower, J., & Kraal, B. (2001). Simultaneous and functional binding of SmpB and EF-Tu-GTP 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
  • 16
    • 0036703022 scopus 로고    scopus 로고
    • Ribosomal protein S1 induces a conformational change of tmRNA; more than one protein S1 per molecule of tmRNA
    • Bordeau, V., & Felden, B. (2002). Ribosomal protein S1 induces a conformational change of tmRNA; more than one protein S1 per molecule of tmRNA. Biochimie, 84, 723-729.
    • (2002) Biochimie , vol.84 , pp. 723-729
    • Bordeau, V.1    Felden, B.2
  • 17
    • 42149193165 scopus 로고    scopus 로고
    • One SmpB molecule accompanies tmRNA during its passage through the ribosomes
    • Bugaeva, E.Y., Shpanchenko, O.V., Felden, B., Isaksson, L.A., & Dontsova, O.A. (2008). One SmpB molecule accompanies tmRNA during its passage through the ribosomes. FEBS Lett., 582, 1532-1536.
    • (2008) FEBS Lett , vol.582 , pp. 1532-1536
    • Bugaeva, E.Y.1    Shpanchenko, O.V.2    Felden, B.3    Isaksson, L.A.4    Dontsova, O.A.5
  • 19
    • 33748510412 scopus 로고    scopus 로고
    • The exosome: a macromolecular cage for controlled RNA degradation
    • Büttner, K., Wenig, K., & Hopfner, K.-P. (2006). The exosome: a macromolecular cage for controlled RNA degradation. Mol Microbiol., 61, 1372-1379.
    • (2006) Mol Microbiol , vol.61 , pp. 1372-1379
    • Büttner, K.1    Wenig, K.2    Hopfner, K.-P.3
  • 20
    • 0344394977 scopus 로고    scopus 로고
    • Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA
    • Cairrão, F. Cruz, A., Mori, H., & Arraiano, C.M. (2003). Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA. Mol Microbiol., 50, 1349-1360.
    • (2003) Mol Microbiol , vol.50 , pp. 1349-1360
    • Cairrão, F.1    Cruz, A.2    Mori, H.3    Arraiano, C.M.4
  • 21
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter, A.P., Clemons, W.M., Brodersen, D.E., Morgan-Warren, R.J., Wimberly, B.T., & Ramakrishnan, V. (2000). Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature, 407, 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 22
    • 0024398325 scopus 로고
    • The gene fo a small stable RNA (10Sa RNA) of Escherichia coli
    • Chauhan, A.K., & Apirion, D. (1989). The gene fo a small stable RNA (10Sa RNA) of Escherichia coli. Mol Microbiol., 3, 1481-1485.
    • (1989) Mol Microbiol , vol.3 , pp. 1481-1485
    • Chauhan, A.K.1    Apirion, D.2
  • 23
    • 34548569082 scopus 로고    scopus 로고
    • Lon protease degrades transfer-messenger RNA-tagged proteins
    • Choy, J.S., Aung, L.L., & Karzai, A.W. (2007). Lon protease degrades transfer-messenger RNA-tagged proteins. J. Bacteriol., 189, 6564-6571.
    • (2007) J. Bacteriol , vol.189 , pp. 6564-6571
    • Choy, J.S.1    Aung, L.L.2    Karzai, A.W.3
  • 24
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen, S.K., Pedersen, K., Hansen, F.G., & Gerdes, K. (2003). Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J. Mol. Biol., 332, 809-819.
    • (2003) J. Mol. Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 25
    • 33745041087 scopus 로고    scopus 로고
    • No mercy for messages that mess with the ribosome
    • Clement, S.L., & Lykke-Andersen, J. (2006). No mercy for messages that mess with the ribosome. Nat. Struct. Mol. Biol., 13, 299-301.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 299-301
    • Clement, S.L.1    Lykke-Andersen, J.2
  • 26
    • 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. (2002). Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli. Mol Microbiol., 45, 745-754.
    • (2002) Mol Microbiol , vol.45 , pp. 745-754
    • Collier, J.1    Binet, E.2    Bouloc, P.3
  • 27
    • 34250729202 scopus 로고    scopus 로고
    • Maturation and degradation of RNA in bacteria
    • Condon, C. (2007). Maturation and degradation of RNA in bacteria. Curr. Opin. Microbiol., 10, 271-278.
    • (2007) Curr. Opin. Microbiol , vol.10 , pp. 271-278
    • Condon, C.1
  • 29
    • 33747145161 scopus 로고    scopus 로고
    • Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis
    • Das, G., & Varshney, U. (2004). Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis. Microbiology, 152, 2191-2195.
    • (2004) Microbiology , vol.152 , pp. 2191-2195
    • Das, G.1    Varshney, U.2
  • 30
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
    • Doma, M.K., & Parker, R. (2006). Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature, 440, 561-564.
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.K.1    Parker, R.2
  • 31
    • 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, D.W. (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
  • 32
    • 33749395736 scopus 로고    scopus 로고
    • Role of Conserved Surface Amino Acids in Binding of SmpB Protein to SsrA RNA
    • Dulebohn, D.P., Cho, H.J., & Karzai, A.W. (2006). Role of Conserved Surface Amino Acids in Binding of SmpB Protein to SsrA RNA. J. Biol. Chem., 281, 28536-28545.
    • (2006) J. Biol. Chem , vol.281 , pp. 28536-28545
    • Dulebohn, D.P.1    Cho, H.J.2    Karzai, A.W.3
  • 35
    • 0032101712 scopus 로고    scopus 로고
    • Presence and location of modified nucleotides in E. 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., & Crain, P.F. (1998). Presence and location of modified nucleotides in E. 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
  • 36
    • 0035845498 scopus 로고    scopus 로고
    • Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
    • Flynn, J.M., Levchenko, I., Seidel, M., Wickner, S.H., Sauer, R.T., & Baker, T.A. (2001). Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. USA, 98, 10584-10589.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10584-10589
    • Flynn, J.M.1    Levchenko, I.2    Seidel, M.3    Wickner, S.H.4    Sauer, R.T.5    Baker, T.A.6
  • 37
    • 0025114689 scopus 로고
    • Enzymatic aminoacylation of an eight-base-pair microhelix with histidine
    • Francklyn, C., & Schimmel, P. (1990). Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc. Natl. Acad. Sci. USA, 87, 8655-8659.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8655-8659
    • Francklyn, C.1    Schimmel, P.2
  • 38
    • 0037155592 scopus 로고    scopus 로고
    • An mRNA surveillance mechanism that eliminates transcripts lacking termination codons
    • Frischmeyer, P.A., van Hoof, A., O'Donnell, K., Guerrerio, A.L., Parker, R., & Dietz, H.C. (2002). An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science, 295, 2258-2261.
    • (2002) Science , vol.295 , pp. 2258-2261
    • Frischmeyer, P.A.1    van Hoof, A.2    O'Donnell, K.3    Guerrerio, A.L.4    Parker, R.5    Dietz, H.C.6
  • 40
    • 0028827880 scopus 로고
    • Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr
    • Fujita, Y., Miwa, Y., Galinier, A., & Deutscher, J. (1995). Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol. Microbiol., 17, 953-960.
    • (1995) Mol. Microbiol , vol.17 , pp. 953-960
    • Fujita, Y.1    Miwa, Y.2    Galinier, A.3    Deutscher, J.4
  • 41
    • 0036715039 scopus 로고    scopus 로고
    • Evolutionary conservation of reactions in translation microbiol
    • Ganoza, M.C., Kiel, M.C., & Aoki, H. (2002). Evolutionary conservation of reactions in translation microbiol. Mol. Biol. Rev., 66, 460-485.
    • (2002) Mol. Biol. Rev , vol.66 , pp. 460-485
    • Ganoza, M.C.1    Kiel, M.C.2    Aoki, H.3
  • 42
    • 33845932593 scopus 로고    scopus 로고
    • Prolyl-tRNAPro in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA
    • Garza-Sánchez, F., Janssen, B.D., & Hayes, C.S. (2006). Prolyl-tRNAPro in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA. J. Biol. Chem., 281, 34258-34268.
    • (2006) J. Biol. Chem , vol.281 , pp. 34258-34268
    • Garza-Sánchez, F.1    Janssen, B.D.2    Hayes, C.S.3
  • 43
    • 42249114323 scopus 로고    scopus 로고
    • Amino acid starvation and colicin D treatment induce A-site mRNA cleavage in Escherichia coli
    • Garza-Sánchez, F., Gin, J.G., & Hayes, C.S. (2008). Amino acid starvation and colicin D treatment induce A-site mRNA cleavage in Escherichia coli. J. Mol. Biol., in press.
    • (2008) J. Mol. Biol
    • Garza-Sánchez, F.1    Gin, J.G.2    Hayes, C.S.3
  • 44
    • 0036566827 scopus 로고    scopus 로고
    • Two-piece tmRNA in cyanobacteria and its structural analysis
    • Gaudin, C., Zhou, X., Williams, K.P., & Felden, B. (2002). Two-piece tmRNA in cyanobacteria and its structural analysis. Nucleic Acids Res., 30, 2025-2030.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2025-2030
    • Gaudin, C.1    Zhou, X.2    Williams, K.P.3    Felden, B.4
  • 45
    • 0035355198 scopus 로고    scopus 로고
    • Transfer RNAAla recognizes transfer-messenger RNA with specificity; a functional complex prior to entering the ribosome?
    • Gillet, R., & Felden, B. (2001a). Transfer RNAAla recognizes transfer-messenger RNA with specificity; a functional complex prior to entering the ribosome? EMBO J., 20, 2966-2976.
    • (2001) EMBO J. , vol.20 , pp. 2966-2976
    • Gillet, R.1    Felden, B.2
  • 46
    • 0035171382 scopus 로고    scopus 로고
    • Emerging views on tmRNA-mediated protein tagging and ribosome rescue
    • Gillet, R., & Felden, B. (2001b). Emerging views on tmRNA-mediated protein tagging and ribosome rescue. Mol. Microbiol., 42, 879-885.
    • (2001) Mol. Microbiol , vol.42 , pp. 879-885
    • Gillet, R.1    Felden, B.2
  • 47
    • 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
  • 48
    • 34247876081 scopus 로고    scopus 로고
    • Ribosome recycling factor and release factor 3 action promotes TnaC-Peptidyl-tRNA dropoff and relieves ribosome stalling during tryptophan induction of tna operon expression in Escherichia coli
    • Gong, M., Cruz-Vera, L.R., & Yanofsky, C. (2007). Ribosome recycling factor and release factor 3 action promotes TnaC-Peptidyl-tRNA dropoff and relieves ribosome stalling during tryptophan induction of tna operon expression in Escherichia coli. J. Bacteriol., 189, 3147-3155.
    • (2007) J. Bacteriol , vol.189 , pp. 3147-3155
    • Gong, M.1    Cruz-Vera, L.R.2    Yanofsky, C.3
  • 49
    • 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. (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
  • 50
    • 0041737720 scopus 로고    scopus 로고
    • Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB
    • Gutmann, S., Haebel, P.W., 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, 5503-5509.
    • (2003) Nature , vol.424 , pp. 5503-5509
    • Gutmann, S.1    Haebel, P.W.2    Metzinger, L.3    Sutter, M.4    Felden, B.5    Ban, N.6
  • 51
    • 1342302787 scopus 로고    scopus 로고
    • Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs
    • Haebel, P.W., Gutmann, S., & Ban, N. (2004). Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs. Curr. Opin. Struct. Biol., 14, 58-65.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 58-65
    • Haebel, P.W.1    Gutmann, S.2    Ban, N.3
  • 52
    • 2942755867 scopus 로고    scopus 로고
    • Pre-binding of small protein B to a stalled ribosome triggers trans-translation
    • Hallier, M., Ivanova, N., Rametti, A., Pavlov, M., Ehrenberg, M., & Felden, B. (2004). Pre-binding of small protein B to a stalled ribosome triggers trans-translation. J. Biol. Chem., 279, 25978-25985.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25978-25985
    • Hallier, M.1    Ivanova, N.2    Rametti, A.3    Pavlov, M.4    Ehrenberg, M.5    Felden, B.6
  • 53
    • 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
  • 54
    • 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
  • 57
    • 0037072794 scopus 로고    scopus 로고
    • Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination
    • Hayes, C.S., Bose, B., & Sauer, R.T. (2002a). Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination. J. Biol. Chem., 277, 33825-33832.
    • (2002) J. Biol. Chem , vol.277 , pp. 33825-33832
    • Hayes, C.S.1    Bose, B.2    Sauer, R.T.3
  • 58
    • 0037133638 scopus 로고    scopus 로고
    • Stop codons preceded by rare arginine codons are efficient determinants of SsrA tagging in Escherichia coli
    • Hayes, C.S., Bose, B., & Sauer, R.T. (2002b). Stop codons preceded by rare arginine codons are efficient determinants of SsrA tagging in Escherichia coli. Proc. Natl. Acad. Sci. USA, 99, 3440-3445.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3440-3445
    • Hayes, C.S.1    Bose, B.2    Sauer, R.T.3
  • 59
    • 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. (2003). Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Mol. Cell, 12, 903-911.
    • (2003) Mol. Cell , vol.12 , pp. 903-911
    • Hayes, C.S.1    Sauer, R.T.2
  • 60
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman, C., Thévenet, D., Bouloc, P., Walker, G.C., & D'Ari, R. (1998). Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev., 12, 1348-1355.
    • (1998) Genes Dev , vol.12 , pp. 1348-1355
    • Herman, C.1    Thévenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 61
    • 0033787385 scopus 로고    scopus 로고
    • Coupling of open reading frames by translational bypassing
    • Herr, A.J., Atkins, J.F., & Gesteland, R.F. (2000). Coupling of open reading frames by translational bypassing. Annu. Rev. Biochem., 69, 343-372.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 343-372
    • Herr, A.J.1    Atkins, J.F.2    Gesteland, R.F.3
  • 63
    • 0038351296 scopus 로고    scopus 로고
    • Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome
    • Heurgue-Hamard, V., Karimi, R., Mora, L., MacDougall, J., Leboeuf, C., Grentzmann, G., Ehrenberg, M., & Buckingham, R.H. (1998). Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome. EMBO J., 17, 808-816.
    • (1998) EMBO J , vol.17 , pp. 808-816
    • Heurgue-Hamard, V.1    Karimi, R.2    Mora, L.3    MacDougall, J.4    Leboeuf, C.5    Grentzmann, G.6    Ehrenberg, M.7    Buckingham, R.H.8
  • 64
    • 0032511223 scopus 로고    scopus 로고
    • A nickel complex cleaves uridines in folded RNA structures: Application to E. coli tmRNA and related engineered molecules
    • Hickerson, R., Watkins-Sims, C.D., Burrows, C.J., Atkins, J.F., Gesteland, R.F., & Felden, B. (1998). A nickel complex cleaves uridines 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.1    Watkins-Sims, C.D.2    Burrows, C.J.3    Atkins, J.F.4    Gesteland, R.F.5    Felden, B.6
  • 65
    • 0023247369 scopus 로고
    • Unusual genetic codes and a novel gene structure for tRNASerAGY in starfish mitochondrial DNA
    • Himeno, H., Masaki, H., Kawai, T., Ohta, T., Kumagai, I., Miura, K., & Watanabe, K. (1987). Unusual genetic codes and a novel gene structure for tRNASerAGY in starfish mitochondrial DNA. Gene, 56, 219-230.
    • (1987) Gene , vol.56 , pp. 219-230
    • Himeno, H.1    Masaki, H.2    Kawai, T.3    Ohta, T.4    Kumagai, I.5    Miura, K.6    Watanabe, K.7
  • 66
    • 0025651675 scopus 로고
    • Conversion of aminoacylation specificity from tRNATyr to tRNASer in vitro
    • Himeno, H., Hasegawa, T., Ueda, T., Watanabe, K., & Shimizu, M. (1990). Conversion of aminoacylation specificity from tRNATyr to tRNASer in vitro. Nucleic Acids Res., 18, 6815-6819.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6815-6819
    • Himeno, H.1    Hasegawa, T.2    Ueda, T.3    Watanabe, K.4    Shimizu, M.5
  • 67
    • 0031584271 scopus 로고    scopus 로고
    • In vitro trans translation mediated by alanine-charged 10Sa RNA
    • Himeno, H., Sato, M., Tadaki, T., Fukushima, M., Ushida, C., & Muto, A. (1997). In vitro trans translation mediated by alanine-charged 10Sa RNA. J. Mol. Biol., 268, 803-808.
    • (1997) J. Mol. Biol , vol.268 , pp. 803-808
    • Himeno, H.1    Sato, M.2    Tadaki, T.3    Fukushima, M.4    Ushida, C.5    Muto, A.6
  • 68
    • 22144462503 scopus 로고    scopus 로고
    • Cell cycle-regulated degradation of tmRNA is controlled by RNase R and SmpB
    • Hong, S.-J., Tran, Q.A., & Keiler, K. (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.3
  • 70
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou, Y.-M., & Schimmel, P. (1988). A simple structural feature is a major determinant of the identity of a transfer RNA. Nature, 333, 140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.-M.1    Schimmel, P.2
  • 71
    • 0034161440 scopus 로고    scopus 로고
    • Charged tmRNA but not tmRNA-mediated proteolysis is essential for Neisseria gonorrhoeae viability
    • Huang, C., Wolfgang, M.C., Withey, J., Koomey, M., & Friedman, D.I. (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
  • 73
    • 0037051891 scopus 로고    scopus 로고
    • Trans-translation mediated by Bacillus subtilis tmRNA
    • Ito, K., Tadaki, T., Lee, S., Takada, K., Muto, A., & Himeno, H. (2002). Trans-translation mediated by Bacillus subtilis tmRNA. FEBS Lett., 516, 245-252.
    • (2002) FEBS Lett. , vol.516 , pp. 245-252
    • Ito, K.1    Tadaki, T.2    Lee, S.3    Takada, K.4    Muto, A.5    Himeno, H.6
  • 75
    • 21344471643 scopus 로고    scopus 로고
    • Mapping the interaction of SmpB with ribosomes by footprinting of ribosomal RNA
    • Ivanova, N., Pavlov, M.Y., Bouakaz, E., Ehrenberg, M., & Schiavone, L.H. (2005). Mapping the interaction of SmpB with ribosomes by footprinting of ribosomal RNA. Nucleic Acids Res., 33, 3529-3539.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3529-3539
    • Ivanova, N.1    Pavlov, M.Y.2    Bouakaz, E.3    Ehrenberg, M.4    Schiavone, L.H.5
  • 77
    • 1642569682 scopus 로고    scopus 로고
    • Loss of the mRNA-like region in mitochondrial tmRNAs of jakobids
    • Jacob, Y., Seif, E., Paquet, P.-O., & Lang, B.F. (2004). Loss of the mRNA-like region in mitochondrial tmRNAs of jakobids. RNA, 10, 605-614.
    • (2004) RNA , vol.10 , pp. 605-614
    • Jacob, Y.1    Seif, E.2    Paquet, P.-O.3    Lang, B.F.4
  • 78
    • 14044265657 scopus 로고    scopus 로고
    • Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form
    • Jacob, Y., Sharkady, S.M., Bhardwaj, K., Sanda, A.A., & Williams, K.P. (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.A.4    Williams, K.P.5
  • 79
    • 0020286552 scopus 로고
    • A small RNA that complements mutants in the RNA processing enzyme ribonuclease P
    • Jain, S.K., Gurevitz, M., & Apirion, D. (1982). A small RNA that complements mutants in the RNA processing enzyme ribonuclease P. J. Mol. Biol., 162, 515-533.
    • (1982) J. Mol. Biol , vol.162 , pp. 515-533
    • Jain, S.K.1    Gurevitz, M.2    Apirion, D.3
  • 80
    • 0034056347 scopus 로고    scopus 로고
    • ssrA (tmRNA) plays a role in Salmonella enterica serovar Typhimurium pathogenesis
    • Julio, S.M., Heithoff, D.M., & Mahan, M.J. (2000). ssrA (tmRNA) plays a role in Salmonella enterica serovar Typhimurium pathogenesis. J. Bacteriol., 182, 1558-1563.
    • (2000) J. Bacteriol , vol.182 , pp. 1558-1563
    • Julio, S.M.1    Heithoff, D.M.2    Mahan, M.J.3
  • 81
    • 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. (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
  • 82
    • 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. (2000). The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue. Nat. Struct. Biol., 7, 449-455.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 83
    • 0035853072 scopus 로고    scopus 로고
    • Protein factors associated with the SsrA-SmpB tagging and ribosome rescue complex
    • Karzai, A.W., & Sauer, R.T. (2001). Protein factors associated with the SsrA-SmpB tagging and ribosome rescue complex. Proc. Natl. Acad. Sci. USA, 98, 3040-3044.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3040-3044
    • Karzai, A.W.1    Sauer, R.T.2
  • 84
    • 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. USA, 103, 16484-16489.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16484-16489
    • Kaur, S.1    Gillet, R.2    Li, W.3    Gursky, R.4    Frank, J.5
  • 85
    • 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. (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
  • 86
    • 0034608854 scopus 로고    scopus 로고
    • tmRNAs that encode proteolysis-inducing tags are found in all known bacterial genomes: A two-piece tmRNA functions in Caulobactor
    • Keiler, K.C., Shapiro, L., & Williams, K.P. (2000). tmRNAs that encode proteolysis-inducing tags are found in all known bacterial genomes: A two-piece tmRNA functions in Caulobactor. Proc. Natl. Acad. Sci. USA, 97, 7778-7783.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7778-7783
    • Keiler, K.C.1    Shapiro, L.2    Williams, K.P.3
  • 87
    • 0037336119 scopus 로고    scopus 로고
    • tmRNA in Caulobacter crescentus is cell cycle regulated by temporally controlled transcription and RNA degradation
    • Keiler, K.C., & Shapiro, L. (2003a). tmRNA in Caulobacter crescentus is cell cycle regulated by temporally controlled transcription and RNA degradation. J. Bacteriol., 185, 1825-1830.
    • (2003) J. Bacteriol , vol.185 , pp. 1825-1830
    • Keiler, K.C.1    Shapiro, L.2
  • 88
    • 0037227964 scopus 로고    scopus 로고
    • tmRNA is required for correct timing of DNA replication in Caulobacter crescentus
    • Keiler, K.C., & Shapiro, L. (2003b). tmRNA is required for correct timing of DNA replication in Caulobacter crescentus. J. Bacteriol., 185, 573-580.
    • (2003) J. Bacteriol , vol.185 , pp. 573-580
    • Keiler, K.C.1    Shapiro, L.2
  • 89
    • 34247165146 scopus 로고    scopus 로고
    • Physiology of tmRNA: what gets tagged and why?
    • Keiler, K.C. (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
  • 91
    • 0029987860 scopus 로고    scopus 로고
    • 10Sa RNA is associated with 70S ribosome particles in Escherichia coli
    • Komine, Y., Kitabatake, M., & Inokuchi, H. (1996). 10Sa RNA is associated with 70S ribosome particles in Escherichia coli. J. Biochem., 119, 463-467.
    • (1996) J. Biochem , vol.119 , pp. 463-467
    • Komine, Y.1    Kitabatake, M.2    Inokuchi, H.3
  • 92
    • 3442899924 scopus 로고    scopus 로고
    • A minimum structure of aminoglycosides that causes an initiation shift of trans-translation
    • Konno, T., Takahashi, T., Kurita, D., Muto, A., & Himeno, H. (2004). A minimum structure of aminoglycosides that causes an initiation shift of trans-translation. Nucleic Acids Res., 32, 4119-4126.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4119-4126
    • Konno, T.1    Takahashi, T.2    Kurita, D.3    Muto, A.4    Himeno, H.5
  • 93
    • 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
  • 94
    • 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
  • 95
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • Lancaster, L., Kiel, M.C., Kaji. A., & Noller, H.F. (2002). Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell, 111, 129-140.
    • (2002) Cell , vol.111 , pp. 129-140
    • Lancaster, L.1    Kiel, M.C.2    Kaji, A.3    Noller, H.F.4
  • 96
    • 0034951396 scopus 로고    scopus 로고
    • Determinants on tmRNA for initiating efficient and precise trans-translation: Some mutations upstream of the tag-encoding sequence of Escherichia coli tmRNA shift the initiation point of trans-translation in vitro
    • Lee, S., Ishii, M., Tadaki, T., Muto, A., & Himeno, H. (2001). Determinants on tmRNA for initiating efficient and precise trans-translation: Some mutations upstream of the tag-encoding sequence of Escherichia coli tmRNA shift the initiation point of trans-translation in vitro. RNA, 7, 999-1012.
    • (2001) RNA , vol.7 , pp. 999-1012
    • Lee, S.1    Ishii, M.2    Tadaki, T.3    Muto, A.4    Himeno, H.5
  • 97
    • 33845916549 scopus 로고    scopus 로고
    • Proteolytic adaptor for transfer-messenger RNA-tagged proteins from alpha-proteobacteria
    • Lessner, F.H., Venters, B.J., & Keiler, K.C. (2007). Proteolytic adaptor for transfer-messenger RNA-tagged proteins from alpha-proteobacteria. J. Bacteriol., 189, 272-275.
    • (2007) J. Bacteriol , vol.189 , pp. 272-275
    • Lessner, F.H.1    Venters, B.J.2    Keiler, K.C.3
  • 98
    • 31044445793 scopus 로고    scopus 로고
    • Protein tagging at rare codons is caused by tmRNA action at the 3' end of nonstop mRNA generated in response to ribosome stalling
    • Li, X., Hirano, R., Tagami, H., & Aiba, H. (2006). Protein tagging at rare codons is caused by tmRNA action at the 3' end of nonstop mRNA generated in response to ribosome stalling. RNA, 12, 248-255.
    • (2006) RNA , vol.12 , pp. 248-255
    • Li, X.1    Hirano, R.2    Tagami, H.3    Aiba, H.4
  • 99
    • 33845685669 scopus 로고    scopus 로고
    • Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli
    • Li, X., Yokota, T., Ito, K., Nakamura, Y., & Aiba, H. (2007). Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli. Mol. Microbiol., 63, 116-126.
    • (2007) Mol. Microbiol , vol.63 , pp. 116-126
    • Li, X.1    Yokota, T.2    Ito, K.3    Nakamura, Y.4    Aiba, H.5
  • 100
    • 41049097536 scopus 로고    scopus 로고
    • Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli
    • Li, X., Yagi, M., Morita, T., & Aiba, H. (2008). Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli. Mol. Microbiol., 68, 462-473.
    • (2008) Mol. Microbiol , vol.68 , pp. 462-473
    • Li, X.1    Yagi, M.2    Morita, T.3    Aiba, H.4
  • 101
    • 0032539857 scopus 로고    scopus 로고
    • 3' Exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Li, Z., Pandit, S. & Deutscher, M.P. (1998). 3' Exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli. Proc. Natl. Acad. Sci. USA, 95, 2856-2861.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2856-2861
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 102
    • 12544252576 scopus 로고    scopus 로고
    • Analysis of recognition of transfer-messenger RNA by the ribosomal decoding center
    • Lim, V.I., & Garber, M.B. (2005). Analysis of recognition of transfer-messenger RNA by the ribosomal decoding center. J. Mol. Biol., 346, 395-398.
    • (2005) J. Mol. Biol , vol.346 , pp. 395-398
    • Lim, V.I.1    Garber, M.B.2
  • 103
    • 0033607239 scopus 로고    scopus 로고
    • RNase E is required for the maturation of ssrA RNA and normal ssrA RNA peptide-tagging activity
    • Lin-Chao, S., Wei, C-L., & Lin, Y.-T. (1999). RNase E is required for the maturation of ssrA RNA and normal ssrA RNA peptide-tagging activity. Proc. Natl. Acad. Sci. USA, 96, 12406-12411.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12406-12411
    • Lin-Chao, S.1    Wei, C.-L.2    Lin, Y.-T.3
  • 104
    • 4544289260 scopus 로고    scopus 로고
    • Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules
    • McGinness, K.E., & Sauer, R.T. (2004). Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules. Proc. Natl. Acad. Sci. USA, 101, 13454-13459.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13454-13459
    • McGinness, K.E.1    Sauer, R.T.2
  • 105
    • 0024279871 scopus 로고
    • Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end
    • McClain, W.H., & Foss, K. (1988). Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end. Science, 240, 793-796.
    • (1988) Science , vol.240 , pp. 793-796
    • McClain, W.H.1    Foss, K.2
  • 106
    • 33845276025 scopus 로고    scopus 로고
    • tmRNA determinants required for facilitating nonstop mRNA decay
    • Mehta, P., Richards, J., & Karzai, A.W. (2006). tmRNA determinants required for facilitating nonstop mRNA decay. RNA, 12, 2187-2198.
    • (2006) RNA , vol.12 , pp. 2187-2198
    • Mehta, P.1    Richards, J.2    Karzai, A.W.3
  • 107
    • 17844381357 scopus 로고    scopus 로고
    • Independent binding sites of small protein B onto transfer-messenger RNA during trans-translation
    • Metzinger, L., Hallier, M., & Felden, B. (2005). Independent binding sites of small protein B onto transfer-messenger RNA during trans-translation. Nucleic Acids Res., 33, 2384-2394.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2384-2394
    • Metzinger, L.1    Hallier, M.2    Felden, B.3
  • 108
    • 42049120450 scopus 로고    scopus 로고
    • SsrA genes of streptomycetes and association of proteins to the tmRNA during development and cellular differentiation
    • Mikulík, k., Paleková, P., Felsberg, J., Bobek, J., Zídková, J., Halada, P. (2008). SsrA genes of streptomycetes and association of proteins to the tmRNA during development and cellular differentiation. Proteomics, 8, 1429-1441.
    • (2008) Proteomics , vol.8 , pp. 1429-1441
    • Mikulík, K.1    Paleková, P.2    Felsberg, J.3    Bobek, J.4    Zídková, J.5    Halada, P.6
  • 109
    • 0034159917 scopus 로고    scopus 로고
    • Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis
    • Miwa, Y., Nakata, A., Ogiwara, A., Yamamoto, M., & Fujita, Y. (2000). Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis. Nucleic Acids Res., 28, 1206-1210.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1206-1210
    • Miwa, Y.1    Nakata, A.2    Ogiwara, A.3    Yamamoto, M.4    Fujita, Y.5
  • 110
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • Moore, S.D., & Sauer, R.T. (2006) The tmRNA system for translational surveillance and ribosome rescue. Annu. Rev. Biochem., 76, 101-124.
    • (2006) Annu. Rev. Biochem , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 111
    • 21844434912 scopus 로고    scopus 로고
    • Analysis of the Escherichia coli Alp phenotype: heat shock induction in ssrA mutants
    • Munavar, H., Zhou, Y., & Gottesman, S. (2005). Analysis of the Escherichia coli Alp phenotype: heat shock induction in ssrA mutants. J. Bacteriol. 187, 4739-4751.
    • (2005) J. Bacteriol , vol.187 , pp. 4739-4751
    • Munavar, H.1    Zhou, Y.2    Gottesman, S.3
  • 112
    • 0030432334 scopus 로고    scopus 로고
    • Structure and function of bacterial 10Sa RNA: trans -translation system
    • Muto, A., Sato, M., Tadaki, T., Fukushima, M., Ushida, C., & Himeno, H. (1996). Structure and function of bacterial 10Sa RNA: trans -translation system. Biochimie, 78, 985-991.
    • (1996) Biochimie , vol.78 , pp. 985-991
    • Muto, A.1    Sato, M.2    Tadaki, T.3    Fukushima, M.4    Ushida, C.5    Himeno, H.6
  • 113
    • 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
  • 114
    • 0033873650 scopus 로고    scopus 로고
    • Requirement of transfer-messenger RNA (tmRNA) 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 (tmRNA) for the growth of Bacillus subtilis under stresses. Genes Cells, 5, 627-636.
    • (2000) Genes Cells , vol.5 , pp. 627-636
    • Muto, A.1    Fujihara, A.2    Ito, K.3    Matsuno, J.4    Ushida, C.5    Himeno, H.6
  • 115
    • 33646517888 scopus 로고    scopus 로고
    • Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A Site for SecM-mediated ribosomal stall
    • Muto, H., Nakatogawa, H., & Ito, K. (2006). Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A Site for SecM-mediated ribosomal stall. Mol. Cell, 22, 545-552.
    • (2006) Mol. Cell , vol.22 , pp. 545-552
    • Muto, H.1    Nakatogawa, H.2    Ito, K.3
  • 116
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • Nakamura, Y., Ito, K., & Isaksson, L.A. (1996). Emerging understanding of translation termination. Cell, 87, 147-150.
    • (1996) Cell , vol.87 , pp. 147-150
    • Nakamura, Y.1    Ito, K.2    Isaksson, L.A.3
  • 117
    • 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
  • 118
    • 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., & 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
  • 119
    • 0033568555 scopus 로고    scopus 로고
    • An NMR and mutational analysis of an RNA pseudoknot of E. coli tmRNA involved in trans -translation
    • Nameki, N., Chattopadhyay, P., Himeno, H., Muto, A., & Kawai, G. (1999b). An NMR and mutational analysis of an RNA pseudoknot of E. coli tmRNA involved in trans -translation. Nucleic Acids Res., 27, 3667-3675.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3667-3675
    • Nameki, N.1    Chattopadhyay, P.2    Himeno, H.3    Muto, A.4    Kawai, G.5
  • 120
    • 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., & Himeno, H. (1999c). 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
  • 121
    • 0034737453 scopus 로고    scopus 로고
    • Three of four pseudoknots in tmRNA are interchangeable and are substitutable with single-stranded RNAs
    • Nameki, N., Tadaki, T., Himeno, H., & Muto, A. (2000). Three of four pseudoknots in tmRNA are interchangeable and are substitutable with single-stranded RNAs. FEBS Lett., 470, 345-349.
    • (2000) FEBS Lett , vol.470 , pp. 345-349
    • Nameki, N.1    Tadaki, T.2    Himeno, H.3    Muto, A.4
  • 124
    • 33646018057 scopus 로고    scopus 로고
    • NMR structure of the Aquifex aeolicus tmRNA pseudoknot PK1: new insights into the recoding event of the ribosomal trans -translation
    • Nonin-Lecomte, S., Felden, B., & Dardel, F. (2006). NMR structure of the Aquifex aeolicus tmRNA pseudoknot PK1: new insights into the recoding event of the ribosomal trans -translation. Nucleic Acids Res., 34, 1847-1853.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1847-1853
    • Nonin-Lecomte, S.1    Felden, B.2    Dardel, F.3
  • 126
    • 0025350539 scopus 로고
    • Location of a gene (ssrA) for a small, stable RNA (10Sa RNA) in the Escherichia coli chromosome
    • Oh, B.K., Chauhan, A.K., Isono, K., & Apirion, D. (1990). Location of a gene (ssrA) for a small, stable RNA (10Sa RNA) in the Escherichia coli chromosome. J. Bacteriol., 172, 4708-4709.
    • (1990) J. Bacteriol , vol.172 , pp. 4708-4709
    • Oh, B.K.1    Chauhan, A.K.2    Isono, K.3    Apirion, D.4
  • 127
    • 84895265706 scopus 로고
    • 10Sa RNA, a small stable RNA of Escherichia coli, is functional
    • Oh, B.K., & Apirion, D. (1991). 10Sa RNA, a small stable RNA of Escherichia coli, is functional. Mol. Gen. Genet., 25, 737-749.
    • (1991) Mol. Gen. Genet , vol.25 , pp. 737-749
    • Oh, B.K.1    Apirion, D.2
  • 128
    • 11144344469 scopus 로고    scopus 로고
    • Contribution of the second OB fold of ribosomal protein S1 from Escherichia coli to the recognition of tmRNA
    • Okada, T., Wower, I.K., Wower, J., Zwieb, C.W., & Kimura, M. (2004). Contribution of the second OB fold of ribosomal protein S1 from Escherichia coli to the recognition of tmRNA. Biosci. Biotechnol. Biochem., 68, 2319-2325.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 2319-2325
    • Okada, T.1    Wower, I.K.2    Wower, J.3    Zwieb, C.W.4    Kimura, M.5
  • 129
    • 33645765576 scopus 로고    scopus 로고
    • A role for the SmpB-SsrA system in Yersinia pseudotuberculosis pathogenesis
    • Okan, N.A., Bliska, J.B., & Karzai, A.W. (2006). A role for the SmpB-SsrA system in Yersinia pseudotuberculosis pathogenesis. PloS Pathog., 2, e6.
    • (2006) PloS Pathog , vol.2
    • Okan, N.A.1    Bliska, J.B.2    Karzai, A.W.3
  • 130
    • 16844379766 scopus 로고    scopus 로고
    • Participation of 3'-to-5' exoribonucleases in the turnover of Bacillus subtilis mRNA
    • Oussenko, I.A., Abe, T., Ujiie, H., Muto, A., & Bechhofer, D.H. (2005). Participation of 3'-to-5' exoribonucleases in the turnover of Bacillus subtilis mRNA. J. Bacteriol., 187, 2758-2767.
    • (2005) J. Bacteriol , vol.187 , pp. 2758-2767
    • Oussenko, I.A.1    Abe, T.2    Ujiie, H.3    Muto, A.4    Bechhofer, D.H.5
  • 131
    • 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. (2003). The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell, 112, 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
  • 132
    • 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
  • 133
    • 33750799914 scopus 로고    scopus 로고
    • The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin, Y., Polacek, N., Vesper, O., Staub, E., Einfeldt, E., Wilson, D.N., & Nierhaus, K.H. (2006). The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell, 127, 721-733.
    • (2006) Cell , vol.127 , pp. 721-733
    • Qin, Y.1    Polacek, N.2    Vesper, O.3    Staub, E.4    Einfeldt, E.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 134
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. (2002). Ribosome structure and the mechanism of translation. Cell, 108, 557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 135
    • 0035964319 scopus 로고    scopus 로고
    • The tRNA function of SsrA contributes to controlling repression of bacteriophage Mu prophage
    • Ranquet, C., Geiselmann, J., & Toussaint, A. (2001). The tRNA function of SsrA contributes to controlling repression of bacteriophage Mu prophage. Proc. Natl. Acad. Sci. USA, 98, 10220-10225.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10220-10225
    • Ranquet, C.1    Geiselmann, J.2    Toussaint, A.3
  • 136
    • 34347406546 scopus 로고    scopus 로고
    • Translational regulation of the Escherichia coli stress factor RpoS: a role for SsrA and Lon
    • Ranquet, C., & Gottesman, S. (2007). Translational regulation of the Escherichia coli stress factor RpoS: a role for SsrA and Lon. J. Bacteriol., 189, 4872-4879.
    • (2007) J. Bacteriol , vol.189 , pp. 4872-4879
    • Ranquet, C.1    Gottesman, S.2
  • 138
    • 0018288428 scopus 로고
    • Characterization of 10S RNA: a new stable molecule from Escherichia coli
    • Ray, B.K., & Apirion, D. (1979). Characterization of 10S RNA: a new stable molecule from Escherichia coli. Mol. Gen. Genet., 74, 25-32.
    • (1979) Mol. Gen. Genet. , vol.74 , pp. 25-32
    • Ray, B.K.1    Apirion, D.2
  • 139
    • 33751358590 scopus 로고    scopus 로고
    • RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner
    • Richards, J., Mehta, P., & Karzai, A.W. (2006). RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner. Mol. Microbiol., 62, 1700-1712.
    • (2006) Mol. Microbiol , vol.62 , pp. 1700-1712
    • Richards, J.1    Mehta, P.2    Karzai, A.W.3
  • 140
    • 0033575660 scopus 로고    scopus 로고
    • SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity
    • Roche, E.D., & 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
  • 141
    • 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. (2001). Identification of endogenous SsrA-tagged proteins reveals tagging at positions corresponding to stop codons. J. Biol. Chem., 276, 28509-28515.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28509-28515
    • Roche, E.D.1    Sauer, R.T.2
  • 142
    • 0032840381 scopus 로고    scopus 로고
    • Aminoacylated tmRNA from Escherichia coli interacts with procaryotic elongation factor Tu
    • Rudinger-Thirion, J., Giegé, R., & Felden, B. (1999). Aminoacylated tmRNA from Escherichia coli interacts with procaryotic elongation factor Tu. RNA, 5, 989-992.
    • (1999) RNA , vol.5 , pp. 989-992
    • Rudinger-Thirion, J.1    Giegé, R.2    Felden, B.3
  • 144
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic
    • Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A., & Liljas, A. (1999). Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science, 286, 2349-2352.
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirokawa, G.3    Kaji, A.4    Liljas, A.5
  • 145
    • 0035834062 scopus 로고    scopus 로고
    • Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA
    • Sengupta, J., Agrawal, R.K., & Frank, J. (2001). Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA. Proc. Natl. Acad. Sci. USA, 98, 11991-11996.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11991-11996
    • Sengupta, J.1    Agrawal, R.K.2    Frank, J.3
  • 146
  • 147
    • 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
  • 148
    • 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
  • 149
    • 34248368843 scopus 로고    scopus 로고
    • The SsrA-SmpB ribosome rescue system is important for growth of Bacillus subtilis at low and high temperature
    • Shin, J.-H., & Price, C.W. (2007). The SsrA-SmpB ribosome rescue system is important for growth of Bacillus subtilis at low and high temperature. J. Bacteriol., 189, 3729-3737.
    • (2007) J. Bacteriol , vol.189 , pp. 3729-3737
    • Shin, J.-H.1    Price, C.W.2
  • 151
    • 11344289875 scopus 로고    scopus 로고
    • A physiological connection between tmRNA and peptidyl-tRNA hydrolase functions in Escherichia coli
    • Singh, N.S., & Varshney, U. (2004). A physiological connection between tmRNA and peptidyl-tRNA hydrolase functions in Escherichia coli. Nucleic Acids Res., 32, 6028-6037.
    • (2004) Nucleic Acids Res , vol.32 , pp. 6028-6037
    • Singh, N.S.1    Varshney, U.2
  • 152
    • 0032190210 scopus 로고    scopus 로고
    • Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and
    • Soma, A., & Himeno, H. (1998). Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae. Nucleic Acids Res., 26, 4374-4381.
    • (1998) Saccharomyces cerevisiae. Nucleic Acids Res. , vol.26 , pp. 4374-4381
    • Soma, A.1    Himeno, H.2
  • 153
    • 35348946378 scopus 로고    scopus 로고
    • Permuted tRNA Genes expressed via a circular RNA intermediate in Cyanidioschyzon merolae
    • Soma, A., Onodera, A., Sugahara, J., Kanai, A., Yachie, N., Tomita, M., Kawamura, F., & Sekine, Y. (2007). Permuted tRNA Genes expressed via a circular RNA intermediate in Cyanidioschyzon merolae. Science, 19, 450-453.
    • (2007) Science , vol.19 , pp. 450-453
    • Soma, A.1    Onodera, A.2    Sugahara, J.3    Kanai, A.4    Yachie, N.5    Tomita, M.6    Kawamura, F.7    Sekine, Y.8
  • 155
    • 0025649203 scopus 로고
    • Maturation of precursor 10Sa RNA in Escherichia coli is a two-step process: the first reaction is catalyzed by RNase III in presence of Mn2+
    • Srivastava, R.K., Miczak, A., & Apirion, D. (1990). Maturation of precursor 10Sa RNA in Escherichia coli is a two-step process: the first reaction is catalyzed by RNase III in presence of Mn2+. Biochimie, 72, 791-802.
    • (1990) Biochimie , vol.72 , pp. 791-802
    • Srivastava, R.K.1    Miczak, A.2    Apirion, D.3
  • 156
    • 0026578439 scopus 로고
    • Characterization of the RNA processing enzyme RNase III from wild type and overexpressing Escherichia coli cells in processing natural RNA substrates
    • Srivastava, R.A., Srivastava, N., & Apirion, D. (1992). Characterization of the RNA processing enzyme RNase III from wild type and overexpressing Escherichia coli cells in processing natural RNA substrates. Int. J. Biochem., 24, 737-749.
    • (1992) Int. J. Biochem , vol.24 , pp. 737-749
    • Srivastava, R.A.1    Srivastava, N.2    Apirion, D.3
  • 158
    • 0037313461 scopus 로고    scopus 로고
    • tmRNA from Thermus thermophilus. Interaction with alanyl-tRNA synthetase and elongation factor Tu
    • Stepanov, V.G., & 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
  • 159
    • 0020671323 scopus 로고
    • Structure and functions of ribosomal protein S1
    • Subramanian, A.R. (1983). Structure and functions of ribosomal protein S1. Prog. Nucleic Acid Res. Mol. Biol., 28, 101-142.
    • (1983) Prog. Nucleic Acid Res. Mol. Biol. , vol.28 , pp. 101-142
    • Subramanian, A.R.1
  • 160
    • 14044271596 scopus 로고    scopus 로고
    • A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans -translation
    • Sundermeier, T.R., Dulebohn, D.P., Cho, H.J., & Karzai, A.W. (2005). A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans -translation. Proc. Natl. Acad. Sci. USA, 102, 2316-2321.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2316-2321
    • Sundermeier, T.R.1    Dulebohn, D.P.2    Cho, H.J.3    Karzai, A.W.4
  • 161
    • 36849093840 scopus 로고    scopus 로고
    • Functional SmpB ribosome interaction require tmRNA
    • Sundermeier, T.R., & Karzai, A.W. (2007). Functional SmpB ribosome interaction 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
  • 162
    • 1242273896 scopus 로고    scopus 로고
    • Nascent-peptide-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. (2002). Nascent-peptide-mediated ribosome stalling at a stop codon induces mRNA cleavage resulting in nonstop mRNA that is recognized by tmRNA. RNA, 10, 378-386.
    • (2002) RNA , vol.10 , pp. 378-386
    • Sunohara, T.1    Jojima, K.2    Yamamoto, Y.3    Inada, T.4    Aiba, H.5
  • 163
    • 1242273896 scopus 로고    scopus 로고
    • Nascent-peptide-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. (2004a). Nascent-peptide-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
  • 164
    • 1842596222 scopus 로고    scopus 로고
    • Ribosome stalling during translation elongation induces cleavage of mRNA being translated in
    • Sunohara, T., Jojima, K., Tagami, H., Inada, T., & Aiba, H. (2004b). Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli. J. Biol. Chem., 279, 15368-15375.
    • (2004) Escherichia coli. J. Biol. Chem , vol.279 , pp. 15368-15375
    • Sunohara, T.1    Jojima, K.2    Tagami, H.3    Inada, T.4    Aiba, H.5
  • 166
    • 0030590849 scopus 로고    scopus 로고
    • Interaction of 10Sa RNA with ribosomes in Escherichia coli
    • Tadaki, T., Fukushima, M., Ushida, C., Himeno, H., & Muto, A. (1996). Interaction of 10Sa RNA with ribosomes in Escherichia coli. FEBS Lett, 399, 223-226.
    • (1996) FEBS Lett , vol.399 , pp. 223-226
    • Tadaki, T.1    Fukushima, M.2    Ushida, C.3    Himeno, H.4    Muto, A.5
  • 167
    • 33947718697 scopus 로고    scopus 로고
    • In vitro trans -translation of Thermus thermophilus: Ribosomal protein S1 is not required for the early stage of trans-translation
    • Takada, K., Takemoto, C., Kawazoe, M., Konno, T., Hanawa-Suetsugu, K., Lee, S., Shirouzu, M., Yokoyama, S., Muto, A., & Himeno, H. (2007). In vitro trans -translation of Thermus thermophilus: Ribosomal protein S1 is not required for the early stage of trans-translation. RNA, 13, 503-510.
    • (2007) RNA , vol.13 , pp. 503-510
    • Takada, K.1    Takemoto, C.2    Kawazoe, M.3    Konno, T.4    Hanawa-Suetsugu, K.5    Lee, S.6    Shirouzu, M.7    Yokoyama, S.8    Muto, A.9    Himeno, H.10
  • 168
    • 0042847384 scopus 로고    scopus 로고
    • Various effects of paromomycin on tmRNA-directed trans -translation
    • Takahashi, T., Konno, T., Muto, A., & Himeno, H. (2003). Various effects of paromomycin on tmRNA-directed trans -translation. J. Biol. Chem., 278, 27672-27680.
    • (2003) J. Biol. Chem , vol.278 , pp. 27672-27680
    • Takahashi, T.1    Konno, T.2    Muto, A.3    Himeno, H.4
  • 170
    • 0030875652 scopus 로고    scopus 로고
    • Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5' leader sequence
    • Tedin, K., Resch, A., & Blasi, U. (1997). Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5' leader sequence. Mol. Microbiol., 25, 189-199.
    • (1997) Mol. Microbiol. , vol.25 , pp. 189-199
    • Tedin, K.1    Resch, A.2    Blasi, U.3
  • 171
    • 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. (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
  • 172
    • 0028040005 scopus 로고
    • Ribosome-messenger recognition in the absence of the Shine-Dalgarno interactions
    • Tzareva, N.V., Makhno, V.I., & Boni, I.V. (1994). Ribosome-messenger recognition in the absence of the Shine-Dalgarno interactions. FEBS Lett., 337, 189-194.
    • (1994) FEBS Lett. , vol.337 , pp. 189-194
    • Tzareva, N.V.1    Makhno, V.I.2    Boni, I.V.3
  • 173
    • 0036112210 scopus 로고    scopus 로고
    • Bacterial SsrA system plays a role in coping with unwanted translational readthrough caused by suppressor tRNAs
    • Ueda, K., Yamamoto, Y., Ogawa, K., Abo, T., Inokuchi, H., & Aiba, H. (2002). Bacterial SsrA system plays a role in coping with unwanted translational readthrough caused by suppressor tRNAs. Genes Cells, 7, 509-519.
    • (2002) Genes Cells , vol.7 , pp. 509-519
    • Ueda, K.1    Yamamoto, Y.2    Ogawa, K.3    Abo, T.4    Inokuchi, H.5    Aiba, H.6
  • 174
    • 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
  • 177
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof, A., Frischmeyer, P.A., Dietz, H.C., & Parker, R. (2002). Exosome-mediated recognition and degradation of mRNAs lacking a termination codon Science, 295, 2262-2264.
    • (2002) Science , vol.295 , pp. 2262-2264
    • van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 180
    • 0037133946 scopus 로고    scopus 로고
    • Small RNAs in bacteria: Diverse regulators of gene expression in response to environmental changes
    • Wasserman, K.M. (2002). Small RNAs in bacteria: Diverse regulators of gene expression in response to environmental changes. Cell, 109, 141-144.
    • (2002) Cell , vol.109 , pp. 141-144
    • Wasserman, K.M.1
  • 181
  • 182
    • 0036567510 scopus 로고    scopus 로고
    • Descent of a split RNA
    • Williams, K.P. (2002). Descent of a split RNA. Nucleic Acids Res, 30, 2025-2030.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2025-2030
    • Williams, K.P.1
  • 183
    • 0029907105 scopus 로고    scopus 로고
    • Phylogenetic analysis of tmRNA secondary structures
    • Williams, K.P., & Bartel, D.P. (1996). Phylogenetic analysis of tmRNA secondary structures. RNA, 2, 1306-1310.
    • (1996) RNA , vol.2 , pp. 1306-1310
    • Williams, K.P.1    Bartel, D.P.2
  • 184
    • 0033215307 scopus 로고    scopus 로고
    • Resuming translation on tmRNA: a unique mode of determining a reading frame
    • Williams, K.P., Martindale, K.A., & Bartel, D.P. (1999). Resuming translation on tmRNA: a unique mode of determining a reading frame. EMBO J., 18, 5423-5433.
    • (1999) EMBO J. , vol.18 , pp. 5423-5433
    • Williams, K.P.1    Martindale, K.A.2    Bartel, D.P.3
  • 185
    • 13444306224 scopus 로고    scopus 로고
    • X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit
    • Wilson, D.N., Schluenzen, F., Harms, J.M., Yoshida, T., Ohkubo, T., Albrecht, R., Buerger, J., Kobayashi, Y., & Fucini, P. (2005). X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit. EMBO J., 24, 251-260.
    • (2005) EMBO J , vol.24 , pp. 251-260
    • Wilson, D.N.1    Schluenzen, F.2    Harms, J.M.3    Yoshida, T.4    Ohkubo, T.5    Albrecht, R.6    Buerger, J.7    Kobayashi, Y.8    Fucini, P.9
  • 186
    • 0032913245 scopus 로고    scopus 로고
    • Analysis of the role of trans-translation in the imm P22 growth in Eschericia coli
    • Withey, J.H., & Friedman, D.I. (1999). Analysis of the role of trans-translation in the imm P22 growth in Eschericia coli. J. Bacteriol., 187, 2148-2157.
    • (1999) J. Bacteriol , vol.187 , pp. 2148-2157
    • Withey, J.H.1    Friedman, D.I.2
  • 187
    • 0242523959 scopus 로고    scopus 로고
    • A salvage pathway for protein structures: tmRNA and trans -translation
    • Withey, J.H., & Friedman, D.I. (2003). A salvage pathway for protein structures: tmRNA and trans -translation. Annu. Rev. Microbiol., 57, 101-123.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 101-123
    • Withey, J.H.1    Friedman, D.I.2
  • 188
    • 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. (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
  • 189
    • 0037118708 scopus 로고    scopus 로고
    • SmpB: a protein that binds to double-stranded segments in tmRNA and tRNA
    • Wower, J., Zwieb, C.W., Hoffman, D.W., & Wower, I.K. (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
  • 190
    • 11144236530 scopus 로고    scopus 로고
    • Contributions of pseudoknots and protein SmpB to the structure and function of tmRNA in trans -translation
    • Wower, I.K., Zwieb, C., & Wower, J. (2004). Contributions of pseudoknots and protein SmpB to the structure and function of tmRNA in trans -translation. J. Biol. Chem. 279, 54202-54209.
    • (2004) J. Biol. Chem , vol.279 , pp. 54202-54209
    • Wower, I.K.1    Zwieb, C.2    Wower, J.3
  • 191
    • 17844398246 scopus 로고    scopus 로고
    • Transfer-messenger RNA unfolds as it transits the ribosome
    • Wower, I.K., Zwieb, C., & Wower, J. (2005). Transfer-messenger RNA unfolds as it transits the ribosome. RNA, 11, 668-673.
    • (2005) RNA , vol.11 , pp. 668-673
    • Wower, I.K.1    Zwieb, C.2    Wower, J.3
  • 192
    • 0037377346 scopus 로고    scopus 로고
    • SsrA-mediated trans -translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs
    • Yamamoto, Y., Sunohara, T., Jojima, K., Inada, T., & Aiba, H. (2003). SsrA-mediated trans -translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs. RNA, 9, 408-418.
    • (2003) RNA , vol.9 , pp. 408-418
    • Yamamoto, Y.1    Sunohara, T.2    Jojima, K.3    Inada, T.4    Aiba, H.5
  • 193
    • 34447528966 scopus 로고    scopus 로고
    • RNA-based regulation of genes of tryptophan synthesis and degradation, in bacteria
    • Yanofsky, C. (2007). RNA-based regulation of genes of tryptophan synthesis and degradation, in bacteria. RNA, 13, 1141-1154.
    • (2007) RNA , vol.13 , pp. 1141-1154
    • Yanofsky, C.1
  • 194
    • 24644446398 scopus 로고    scopus 로고
    • Ribo-gnome: The big world of small RNAs
    • Zamore, P.D., & Haley, B. (2005). Ribo-gnome: The big world of small RNAs. Science, 309, 1519-1524.
    • (2005) Science , vol.309 , pp. 1519-1524
    • Zamore, P.D.1    Haley, B.2
  • 196
    • 0033562579 scopus 로고    scopus 로고
    • Comparative sequence analysis of tmRNA
    • Zwieb, C., Wower, I., & Wower, J. (1999). Comparative sequence analysis of tmRNA. Nucleic Acids Res., 27, 2063-2071.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2063-2071
    • Zwieb, C.1    Wower, I.2    Wower, J.3
  • 197
    • 0035859794 scopus 로고    scopus 로고
    • Three-dimensional folding of the tRNA-like domain of Escherichia coli tmRNA
    • Zwieb, C., Guven, S.A., Wower, I.K., & Wower, J. (2003). Three-dimensional folding of the tRNA-like domain of Escherichia coli tmRNA. Biochemistry, 40, 9587-9595.
    • (2003) Biochemistry , vol.40 , pp. 9587-9595
    • Zwieb, C.1    Guven, S.A.2    Wower, I.K.3    Wower, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.