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Volumn 5, Issue APR, 2014, Pages

The fail-safe system to rescue the stalled ribosomes in Escherichia coli

Author keywords

ArfA; ArfB; Escherichia coli; Ribosome rescue; Trans translation

Indexed keywords

AMINOACYL TRANSFER RNA; EXORIBONUCLEASE; OLIGODEOXYRIBONUCLEOTIDE; PUROMYCIN; RIBOSOME RESCUE FACTOR; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84899682599     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00156     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0035985042 scopus 로고    scopus 로고
    • SsrA-mediated protein tagging in the presence of miscoding drugs and its physiological role in Escherichia coli
    • doi: 10.1046/j.1365-2443.2002.00549.x
    • Abo, T., Ueda, K., Sunohara, T., Ogawa, K., and 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. doi: 10.1046/j.1365-2443.2002.00549.x
    • (2002) Genes Cells , vol.7 , pp. 629-638
    • Abo, T.1    Ueda, K.2    Sunohara, T.3    Ogawa, K.4    Aiba, H.5
  • 2
    • 84857768741 scopus 로고    scopus 로고
    • The tmRNA-tagging mechanism and the control of gene expression: a review
    • doi: 10.1002/wrna.48
    • Barends, S., Kraal, B., and van Wezel, G. P. (2011). The tmRNA-tagging mechanism and the control of gene expression: a review. Wiley Interdiscip. Rev. RNA 2, 233-246. doi: 10.1002/wrna.48
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 233-246
    • Barends, S.1    Kraal, B.2    van Wezel, G.P.3
  • 3
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • doi: 10.1111/j.1365-2958.2004.04063.x
    • Bernhardt, T. G., and de Boer, P. A. (2004). Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol. Microbiol. 52, 1255-1269. doi: 10.1111/j.1365-2958.2004.04063.x
    • (2004) Mol. Microbiol. , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 4
    • 84867044295 scopus 로고    scopus 로고
    • ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli
    • doi: 10.1111/j.1365-2958.2012.08190.x
    • Chadani, Y., Ito, K., Kutsukake, K., and Abo, T. (2012). ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli. Mol. Microbiol. 86, 37-50. doi: 10.1111/j.1365-2958.2012.08190.x
    • (2012) Mol. Microbiol. , vol.86 , pp. 37-50
    • Chadani, Y.1    Ito, K.2    Kutsukake, K.3    Abo, T.4
  • 5
    • 79955008757 scopus 로고    scopus 로고
    • Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways
    • doi: 10.1111/j.1365-2958.2011.07607.x
    • Chadani, Y., Ono, K., Kutsukake, K., and Abo, T. (2011a). Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways. Mol. Microbiol. 80, 772-785. doi: 10.1111/j.1365-2958.2011.07607.x
    • (2011) Mol. Microbiol. , vol.80 , pp. 772-785
    • Chadani, Y.1    Ono, K.2    Kutsukake, K.3    Abo, T.4
  • 6
    • 80053318072 scopus 로고    scopus 로고
    • trans-translation-mediated tight regulation of the expression of the alternative ribosome-rescue factor ArfA in Escherichia coli
    • doi: 10.1266/ggs.86.151
    • Chadani, Y., Matsumoto, E., Aso, H., Wada, T., Kutsukake, K., Sutou, S., et al. (2011b). trans-translation-mediated tight regulation of the expression of the alternative ribosome-rescue factor ArfA in Escherichia coli. Genes Genet. Syst. 86, 151-163. doi: 10.1266/ggs.86.151
    • (2011) Genes Genet. Syst. , vol.86 , pp. 151-163
    • Chadani, Y.1    Matsumoto, E.2    Aso, H.3    Wada, T.4    Kutsukake, K.5    Sutou, S.6
  • 7
    • 78349300881 scopus 로고    scopus 로고
    • Ribosome rescue by Escherichia coli ArfA (YhdL) in the absence of trans-translation system
    • doi: 10.1111/j.1365-2958.2010.07375.x
    • Chadani, Y., Ono, K., Ozawa, S., Takahashi, Y., Takai, K., Nanamiya, H., et al. (2010). Ribosome rescue by Escherichia coli ArfA (YhdL) in the absence of trans-translation system. Mol. Microbiol. 78, 796-808. doi: 10.1111/j.1365-2958.2010.07375.x
    • (2010) Mol. Microbiol. , vol.78 , pp. 796-808
    • Chadani, Y.1    Ono, K.2    Ozawa, S.3    Takahashi, Y.4    Takai, K.5    Nanamiya, H.6
  • 8
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • doi: 10.1046/j.1365-2958.2003.03512.x
    • Christensen, S. K., and Gerdes, K. (2003). RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol. Microbiol. 48, 1389-1400. doi: 10.1046/j.1365-2958.2003.03512.x
    • (2003) Mol. Microbiol. , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 9
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • doi: 10.1016/S0022-2836(03)00922-7
    • Christensen, S. K., Pedersen, K., Hansen, F. G., and 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. doi: 10.1016/S0022-2836(03)00922-7
    • (2003) J. Mol. Biol. , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 10
    • 84871921644 scopus 로고    scopus 로고
    • EF-P is essential for rapid synthesis of proteins containing consecutive proline residues
    • doi: 10.1126/science.1229017
    • Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., and Rodnina, M. V. (2013). EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339, 85-88. doi: 10.1126/science.1229017
    • (2013) Science , vol.339 , pp. 85-88
    • Doerfel, L.K.1    Wohlgemuth, I.2    Kothe, C.3    Peske, F.4    Urlaub, H.5    Rodnina, M.V.6
  • 11
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • doi: 10.1017/S135583829999043X
    • Frolova, L. Y., Tsivkovskii, R. Y., Sivolobova, G. F., Oparina, N. Y., Serpinsky, O. I., Blinov, V. M., et al. (1999). Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5, 1014-1020. doi: 10.1017/S135583829999043X
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6
  • 12
    • 84858309380 scopus 로고    scopus 로고
    • Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome
    • doi: 10.1126/science.1217443
    • Gagnon, M. G., Seetharaman, S. V., Bulkley, D., and Steitz, T. A. (2012). Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science 335, 1370-1372. doi: 10.1126/science.1217443
    • (2012) Science , vol.335 , pp. 1370-1372
    • Gagnon, M.G.1    Seetharaman, S.V.2    Bulkley, D.3    Steitz, T.A.4
  • 13
    • 79957496565 scopus 로고    scopus 로고
    • tmRNA regulates synthesis of the ArfA ribosome rescue factor
    • doi: 10.1111/j.1365-2958.2011.07638.x
    • Garza-Sánchez, F., Schaub, R. E., Janssen, B. D., and Hayes, C. S. (2011). tmRNA regulates synthesis of the ArfA ribosome rescue factor. Mol. Microbiol. 80, 1204-1219. doi: 10.1111/j.1365-2958.2011.07638.x
    • (2011) Mol. Microbiol. , vol.80 , pp. 1204-1219
    • Garza-Sánchez, F.1    Schaub, R.E.2    Janssen, B.D.3    Hayes, C.S.4
  • 14
    • 70350146494 scopus 로고    scopus 로고
    • RNase II is important for A-site mRNA cleavage during ribosome pausing
    • doi: 10.1111/j.1365-2958.2009.06813.x
    • Garza-Sánchez, F., Shoji, S., Fredrick, K., and Hayes, C. S. (2009). RNase II is important for A-site mRNA cleavage during ribosome pausing. Mol. Microbiol. 73, 882-897. doi: 10.1111/j.1365-2958.2009.06813.x
    • (2009) Mol. Microbiol. , vol.73 , pp. 882-897
    • Garza-Sánchez, F.1    Shoji, S.2    Fredrick, K.3    Hayes, C.S.4
  • 15
    • 84880736920 scopus 로고    scopus 로고
    • The task force that rescues stalled ribosomes in bacteria
    • doi: 10.1016/j.tibs.2013.06.002
    • Giudice, E., and Gillet, R. (2013). The task force that rescues stalled ribosomes in bacteria. Trends Biochem. Sci. 38, 403-411. doi: 10.1016/j.tibs.2013.06.002
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 403-411
    • Giudice, E.1    Gillet, R.2
  • 16
    • 78349313687 scopus 로고    scopus 로고
    • Solution structure of the catalytic domain of the mitochondrial protein ICT1 that is essential for cell vitality
    • doi: 10.1016/j.jmb.2010.09.033
    • Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., et al. (2010). Solution structure of the catalytic domain of the mitochondrial protein ICT1 that is essential for cell vitality. J. Mol. Biol. 404, 260-273. doi: 10.1016/j.jmb.2010.09.033
    • (2010) J. Mol. Biol. , vol.404 , pp. 260-273
    • Handa, Y.1    Hikawa, Y.2    Tochio, N.3    Kogure, H.4    Inoue, M.5    Koshiba, S.6
  • 17
    • 79953142009 scopus 로고    scopus 로고
    • YaeJ is a novel ribosome-associated protein in Escherichia coli that can hydrolyze peptidyl-tRNA on stalled ribosomes
    • doi: 10.1093/nar/gkq1097
    • Handa, Y., Inaho, N., and Nameki, N. (2011). YaeJ is a novel ribosome-associated protein in Escherichia coli that can hydrolyze peptidyl-tRNA on stalled ribosomes. Nucleic Acids Res. 39, 1739-1748. doi: 10.1093/nar/gkq1097
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1739-1748
    • Handa, Y.1    Inaho, N.2    Nameki, N.3
  • 18
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • doi: 10.1073/pnas.94.10.4937
    • Hanes, J., and Plückthun, A. (1997). In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. U.S.A. 94, 4937-4942. doi: 10.1073/pnas.94.10.4937
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 19
    • 71549151293 scopus 로고    scopus 로고
    • Beyond ribosome rescue: tmRNA and co-translational processes
    • doi: 10.1016/j.febslet.2009.11.023
    • Hayes, C. S., and Keiler, K. C. (2010). Beyond ribosome rescue: tmRNA and co-translational processes. FEBS Lett. 584, 413-419. doi: 10.1016/j.febslet.2009.11.023
    • (2010) FEBS Lett. , vol.584 , pp. 413-419
    • Hayes, C.S.1    Keiler, K.C.2
  • 20
    • 0034161440 scopus 로고    scopus 로고
    • Charged tmRNA but not tmRNA-mediated proteolysis is essential for Neisseria gonorrhoeae viability
    • doi: 10.1093/emboj/19.5.1098
    • Huang, C., Wolfgang, M. C., Withey, J., Koomey, M., and Friedman, D. I. (2000). Charged tmRNA but not tmRNA-mediated proteolysis is essential for Neisseria gonorrhoeae viability. EMBO J. 19, 1098-1107. doi: 10.1093/emboj/19.5.1098
    • (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
  • 21
    • 84894213782 scopus 로고    scopus 로고
    • A-site mRNA cleavage is not required for tmRNA-mediated ssrA-peptide tagging
    • doi: 10.1371/journal.pone.0081319
    • Janssen, B. D., Garza-Sánchez, F., and Hayes, C. S. (2013). A-site mRNA cleavage is not required for tmRNA-mediated ssrA-peptide tagging. PLoS ONE 8:e81319. doi: 10.1371/journal.pone.0081319
    • (2013) PLoS ONE , vol.8
    • Janssen, B.D.1    Garza-Sánchez, F.2    Hayes, C.S.3
  • 22
    • 84855896806 scopus 로고    scopus 로고
    • The tmRNA ribosome-rescue system
    • doi: 10.1016/B978-0-12-386497-0.00005-0
    • Janssen, B. D., and Hayes, C. S. (2012). The tmRNA ribosome-rescue system. Adv. Protein Chem. Struct. Biol. 86, 151-191. doi: 10.1016/B978-0-12-386497-0.00005-0
    • (2012) Adv. Protein Chem. Struct. Biol. , vol.86 , pp. 151-191
    • Janssen, B.D.1    Hayes, C.S.2
  • 23
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • doi: 10.1093/emboj/18.13.3793
    • Karzai, A., Susskind, M., and Sauer, R. (1999). SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J. 18, 3793-3799. doi: 10.1093/emboj/18.13.3793
    • (1999) EMBO J. , vol.18 , pp. 3793-3799
    • Karzai, A.1    Susskind, M.2    Sauer, R.3
  • 24
    • 53849117142 scopus 로고    scopus 로고
    • Biology of trans-translation
    • doi: 10.1146/annurev.micro.62.081307.162948
    • Keiler, K. C. (2008). Biology of trans-translation. Annu. Rev. Microbiol. 62, 133-151. doi: 10.1146/annurev.micro.62.081307.162948
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 133-151
    • Keiler, K.C.1
  • 25
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of protein synthesized from damaged messenger RNA
    • doi: 10.1126/science.271.5251.990
    • Keiler, K. C., Weller, P. R., and Sauer, R. T. (1996). Role of a peptide tagging system in degradation of protein synthesized from damaged messenger RNA. Science 271, 990-993. doi: 10.1126/science.271.5251.990
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Weller, P.R.2    Sauer, R.T.3
  • 26
    • 38849132849 scopus 로고    scopus 로고
    • kinA mRNA is missing a stop codon in the undomesticated Bacillus subtilis strain ATCC 6051
    • doi: 10.1099/mic.0.2007/011783-0
    • Kobayashi, K., Kuwana, R., and Takamatsu, H. (2008). kinA mRNA is missing a stop codon in the undomesticated Bacillus subtilis strain ATCC 6051. Microbiology 154, 54-63. doi: 10.1099/mic.0.2007/011783-0
    • (2008) Microbiology , vol.154 , pp. 54-63
    • Kobayashi, K.1    Kuwana, R.2    Takamatsu, H.3
  • 27
    • 84898029330 scopus 로고    scopus 로고
    • Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ
    • doi: 10.1093/nar/gkt1280
    • Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K., et al. (2014). Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ. Nucleic Acids Res. 42, 3152-3163. doi: 10.1093/nar/gkt1280
    • (2014) Nucleic Acids Res. , vol.42 , pp. 3152-3163
    • Kogure, H.1    Handa, Y.2    Nagata, M.3    Kanai, N.4    Güntert, P.5    Kubota, K.6
  • 28
    • 0028124122 scopus 로고
    • A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli
    • doi: 10.1073/pnas.91.20.9223
    • Komine, Y., Kitabatake, M., Yokogawa, T., Nishikawa, K., and Inokuchi, H. (1994). A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 91, 9223-9227. doi: 10.1073/pnas.91.20.9223
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9223-9227
    • Komine, Y.1    Kitabatake, M.2    Yokogawa, T.3    Nishikawa, K.4    Inokuchi, H.5
  • 29
    • 66749121220 scopus 로고    scopus 로고
    • Analysis of nonstop mRNA translation in the absence of tmRNA in Escherichia coli
    • doi: 10.1111/j.1365-2443.2009.01304.x
    • Kuroha, K., Horiguchi, N., Aiba, H., and Inada, T. (2009). Analysis of nonstop mRNA translation in the absence of tmRNA in Escherichia coli. Genes Cells 14, 739-749. doi: 10.1111/j.1365-2443.2009.01304.x
    • (2009) Genes Cells , vol.14 , pp. 739-749
    • Kuroha, K.1    Horiguchi, N.2    Aiba, H.3    Inada, T.4
  • 30
    • 41049097536 scopus 로고    scopus 로고
    • Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli
    • doi: 10.1111/j.1365-2958.2008.06167.x
    • Li, X., Yogi, M., Morita, T., and Aiba, H. (2008). Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli. Mol. Microbiol. 68, 462-473. doi: 10.1111/j.1365-2958.2008.06167.x
    • (2008) Mol. Microbiol. , vol.68 , pp. 462-473
    • Li, X.1    Yogi, M.2    Morita, T.3    Aiba, H.4
  • 31
    • 25444509798 scopus 로고    scopus 로고
    • tmRNA decreases the bacterial activity of aminoglycosides and susceptibility to inhibitors of cell wall synthesis
    • doi: 10.4161/rna.2.2.2020
    • Luidalepp, H., Hallier, M., Felden, B., and Tenson, T. (2005). tmRNA decreases the bacterial activity of aminoglycosides and susceptibility to inhibitors of cell wall synthesis. RNA Biol. 2, 70-74. doi: 10.4161/rna.2.2.2020
    • (2005) RNA Biol. , vol.2 , pp. 70-74
    • Luidalepp, H.1    Hallier, M.2    Felden, B.3    Tenson, T.4
  • 32
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • doi: 10.1146/annurev.biochem.75.103004.142733
    • Moore, S. D., and Sauer, R. T. (2007). The tmRNA system for translational surveillance and ribosome rescue. Annu. Rev. Biochem. 76, 101-124. doi: 10.1146/annurev.biochem.75.103004.142733
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 33
    • 0034893387 scopus 로고    scopus 로고
    • Temperature-sensitive mutations in various genes of Escherichia coli K12 can be suppressed by the ssrA gene for 10Sa RNA (tmRNA)
    • doi: 10.1007/s004380100453
    • Nakano, H., Goto, S., Nakayashiki, T., and Inokuchi, H. (2001). Temperature-sensitive mutations in various genes of Escherichia coli K12 can be suppressed by the ssrA gene for 10Sa RNA (tmRNA). Mol. Genet. Genomics 265, 615-621. doi: 10.1007/s004380100453
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 615-621
    • Nakano, H.1    Goto, S.2    Nakayashiki, T.3    Inokuchi, H.4
  • 34
    • 65949086018 scopus 로고    scopus 로고
    • Suppression by enhanced RpoE activity of the temperature-sensitive phenotype of a degP ssrA double mutant in Escherichia coli
    • doi: 10.1266/ggs.84.15
    • Ono, K., Kutsukake, K., and Abo, T. (2009). Suppression by enhanced RpoE activity of the temperature-sensitive phenotype of a degP ssrA double mutant in Escherichia coli. Genes Genet. Syst. 84, 15-24. doi: 10.1266/ggs.84.15
    • (2009) Genes Genet. Syst. , vol.84 , pp. 15-24
    • Ono, K.1    Kutsukake, K.2    Abo, T.3
  • 35
    • 0025044578 scopus 로고
    • Carboxy-terminal determinants of intracellular protein degradation
    • doi: 10.1101/gad.4.2.277
    • Parsell, D. A., Silber, K. R., and Sauer, R. T. (1990). Carboxy-terminal determinants of intracellular protein degradation. Genes Dev. 4, 277-286. doi: 10.1101/gad.4.2.277
    • (1990) Genes Dev. , vol.4 , pp. 277-286
    • Parsell, D.A.1    Silber, K.R.2    Sauer, R.T.3
  • 36
    • 79952769630 scopus 로고    scopus 로고
    • Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations
    • doi: 10.1073/pnas.1012994108
    • Pech, M., Karim, Z., Yamamoto, H., Kitakawa, M., Qin, Y., and Nierhaus, K. H. (2011). Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations. Proc. Natl. Acad. Sci. U.S.A. 108, 3199-3203. doi: 10.1073/pnas.1012994108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3199-3203
    • Pech, M.1    Karim, Z.2    Yamamoto, H.3    Kitakawa, M.4    Qin, Y.5    Nierhaus, K.H.6
  • 37
    • 84867063728 scopus 로고    scopus 로고
    • Three mechanisms in Escherichia coli rescue ribosomes stalled on non-stop mRNAs: one of them requires release factor 2
    • doi: 10.1111/j.1365-2958.2012.08207.x
    • Pech, M., and Nierhaus, K. H. (2012). Three mechanisms in Escherichia coli rescue ribosomes stalled on non-stop mRNAs: one of them requires release factor 2. Mol. Microbiol. 86, 6-9. doi: 10.1111/j.1365-2958.2012.08207.x
    • (2012) Mol. Microbiol. , vol.86 , pp. 6-9
    • Pech, M.1    Nierhaus, K.H.2
  • 38
    • 84874378359 scopus 로고    scopus 로고
    • tmRNA is essential in Shigella flexneri
    • doi: 10.1371/journal.pone.0057537
    • Ramadoss, N. S., Zhou, X., and Keiler, K. C. (2013). tmRNA is essential in Shigella flexneri. PLoS ONE 8:e57537. doi: 10.1371/journal.pone.0057537
    • (2013) PLoS ONE , vol.8
    • Ramadoss, N.S.1    Zhou, X.2    Keiler, K.C.3
  • 39
    • 0025649204 scopus 로고
    • RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression
    • doi: 10.1016/0300-9084(90)90192-J
    • Régnier, P., and Grunberg-Manago, M. (1990). RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression. Biochimie 72, 825-834. doi: 10.1016/0300-9084(90)90192-J
    • (1990) Biochimie , vol.72 , pp. 825-834
    • Régnier, P.1    Grunberg-Manago, M.2
  • 40
    • 77949547496 scopus 로고    scopus 로고
    • A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome
    • doi: 10.1038/emboj.2010.14
    • Richter, R., Rorbach, J., Pajak, A., Smith, P. M., Wessels, H. J., Huynen, M. A., et al. (2010). A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome. EMBO J. 29, 1116-1125. doi: 10.1038/emboj.2010.14
    • (2010) EMBO J. , vol.29 , pp. 1116-1125
    • Richter, R.1    Rorbach, J.2    Pajak, A.3    Smith, P.M.4    Wessels, H.J.5    Huynen, M.A.6
  • 41
    • 0038012848 scopus 로고    scopus 로고
    • Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF 2
    • doi: 10.1074/jbc.M211024200
    • Scarlett, D. J., McCaughan, K. K., Wilson, D. N., and Tate, W. P. (2003). Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2. J. Biol. Chem. 278, 15095-15104. doi: 10.1074/jbc.M211024200
    • (2003) J. Biol. Chem. , vol.278 , pp. 15095-15104
    • Scarlett, D.J.1    McCaughan, K.K.2    Wilson, D.N.3    Tate, W.P.4
  • 42
    • 84867267912 scopus 로고    scopus 로고
    • ArfA recruits RF2 into stalled ribosomes
    • doi: 10.1016/j.jmb.2012.08.007
    • Shimizu, Y. (2012). ArfA recruits RF2 into stalled ribosomes. J. Mol. Biol. 423, 624-631. doi: 10.1016/j.jmb.2012.08.007
    • (2012) J. Mol. Biol. , vol.423 , pp. 624-631
    • Shimizu, Y.1
  • 43
    • 44949251773 scopus 로고    scopus 로고
    • Recycling of ribosomal complexes stalled at the step of elongation in Escherichia coli
    • doi: 10.1016/j.jmb.2008.05.033
    • Singh, N. S., Ahmad, R., Sangeetha, R., and Varshney, U. (2008). Recycling of ribosomal complexes stalled at the step of elongation in Escherichia coli. J. Mol. Biol. 380, 451-464. doi: 10.1016/j.jmb.2008.05.033
    • (2008) J. Mol. Biol. , vol.380 , pp. 451-464
    • Singh, N.S.1    Ahmad, R.2    Sangeetha, R.3    Varshney, U.4
  • 44
    • 84871918588 scopus 로고    scopus 로고
    • Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches
    • doi: 10.1126/science.1228985
    • Ude, S., Lassak, J., Starosta, A. L., Kraxenberger, T., Wilson, D. N., and Jung, K. (2013). Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science 339, 82-85. doi: 10.1126/science.1228985
    • (2013) Science , vol.339 , pp. 82-85
    • Ude, S.1    Lassak, J.2    Starosta, A.L.3    Kraxenberger, T.4    Wilson, D.N.5    Jung, K.6
  • 45
    • 84858298050 scopus 로고    scopus 로고
    • Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons
    • doi: 10.1016/j.jmb.2012.02.008
    • Vivanco-Domínguez, S., Bueno-Martínez, J., León-Avila, G., Iwakura, N., Kaji, A., Kaji, H., et al. (2012). Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons. J. Mol. Biol. 417, 425-439. doi: 10.1016/j.jmb.2012.02.008
    • (2012) J. Mol. Biol. , vol.417 , pp. 425-439
    • Vivanco-Domínguez, S.1    Bueno-Martínez, J.2    León-Avila, G.3    Iwakura, N.4    Kaji, A.5    Kaji, H.6
  • 46
    • 0037377346 scopus 로고    scopus 로고
    • SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs
    • doi: 10.1261/rna.2174803
    • Yamamoto, Y., Sunohara, T., Jojima, K., Inada, T., and Aiba, H. (2003). SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs. RNA 9, 408-418. doi: 10.1261/rna.2174803
    • (2003) RNA , vol.9 , pp. 408-418
    • Yamamoto, Y.1    Sunohara, T.2    Jojima, K.3    Inada, T.4    Aiba, H.5
  • 47
    • 53849146066 scopus 로고    scopus 로고
    • Peptide release on the ribosome: mechanism and implications for translational control
    • doi: 10.1146/annurev.micro.61.080706.093323
    • Youngman, E. M., McDonald, M. E., and Green, R. (2008). Peptide release on the ribosome: mechanism and implications for translational control. Annu. Rev. Microbiol. 62, 353-373. doi: 10.1146/annurev.micro.61.080706.093323
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 353-373
    • Youngman, E.M.1    McDonald, M.E.2    Green, R.3
  • 48
    • 58149354143 scopus 로고    scopus 로고
    • Quality control by the ribosome following peptide bond formation
    • doi: 10.1038/nature07582
    • Zaher, H. S., and Green, R. (2009). Quality control by the ribosome following peptide bond formation. Nature 457, 161-166. doi: 10.1038/nature07582
    • (2009) Nature , vol.457 , pp. 161-166
    • Zaher, H.S.1    Green, R.2


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