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Volumn 288, Issue 48, 2013, Pages 34791-34798

Ribosomes regulate the stability and action of the exoribonuclease RNase R

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR HOMEOSTASIS; FREEFORMS; REGULATORY MECHANISM; RIBOSOMAL PROTEINS; RNA METABOLISMS; SECONDARY STRUCTURES;

EID: 84889016452     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.519553     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 0242496945 scopus 로고    scopus 로고
    • Degradation of stable RNA in bacteria
    • Deutscher, M. P. (2003) Degradation of stable RNA in bacteria. J. Biol. Chem. 278, 45041-45044
    • (2003) J. Biol. Chem , vol.278 , pp. 45041-45044
    • Deutscher, M.P.1
  • 2
    • 32644435694 scopus 로고    scopus 로고
    • Degradation of RNA in bacteria. Comparison of mRNA and stable RNA
    • Deutscher, M. P. (2006) Degradation of RNA in bacteria. Comparison of mRNA and stable RNA. Nucleic Acids Res. 34, 659-666
    • (2006) Nucleic Acids Res , vol.34 , pp. 659-666
    • Deutscher, M.P.1
  • 5
    • 64049095465 scopus 로고    scopus 로고
    • Maturation and degradation of ribosomal RNA in bacteria
    • Deutscher, M. P. (2009) Maturation and degradation of ribosomal RNA in bacteria. Prog. Mol. Biol. Transl. Sci. 85, 369-391
    • (2009) Prog. Mol. Biol. Transl. Sci , vol.85 , pp. 369-391
    • Deutscher, M.P.1
  • 6
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies. Structural analysis and phylogenetic distribution
    • Zuo, Y., and Deutscher, M. P. (2001) Exoribonuclease superfamilies. Structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026
    • (2001) Nucleic Acids Res , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 7
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • Cheng, Z. F., and Deutscher, M. P. (2002) Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277, 21624-21629
    • (2002) J. Biol. Chem , vol.277 , pp. 21624-21629
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 8
    • 0032486392 scopus 로고    scopus 로고
    • The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R
    • Cheng, Z. F., Zuo, Y., Li, Z., Rudd, K. E., and Deutscher, M. P. (1998) The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J. Biol. Chem. 273, 14077-14080
    • (1998) J. Biol. Chem , vol.273 , pp. 14077-14080
    • Cheng, Z.F.1    Zuo, Y.2    Li, Z.3    Rudd, K.E.4    Deutscher, M.P.5
  • 9
    • 12344330602 scopus 로고    scopus 로고
    • An important role for RNase R in mRNA decay
    • Cheng, Z. F., and Deutscher, M. P. (2005) An important role for RNase R in mRNA decay. Mol. Cell 17, 313-318
    • (2005) Mol. Cell , vol.17 , pp. 313-318
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 10
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • Vincent, H. A., and Deutscher, M. P. (2006) Substrate recognition and catalysis by the exoribonuclease RNase R. J. Biol. Chem. 281, 29769- 29775
    • (2006) J. Biol. Chem , vol.281 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 11
    • 58649092877 scopus 로고    scopus 로고
    • The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA
    • Vincent, H. A., and Deutscher, M. P. (2009) The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA. J. Biol. Chem. 284, 486-494
    • (2009) J. Biol. Chem , vol.284 , pp. 486-494
    • Vincent, H.A.1    Deutscher, M.P.2
  • 12
    • 62049085767 scopus 로고    scopus 로고
    • Insights into how RNase R degrades structured RNA. Analysis of the nuclease domain
    • Vincent, H. A., and Deutscher, M. P. (2009) Insights into how RNase R degrades structured RNA. Analysis of the nuclease domain. J. Mol. Biol. 387, 570-583
    • (2009) J. Mol. Biol , vol.387 , pp. 570-583
    • Vincent, H.A.1    Deutscher, M.P.2
  • 13
    • 27144467868 scopus 로고    scopus 로고
    • Elevation of RNase R in response to multiple stress conditions
    • Chen, C., and Deutscher, M. P. (2005) Elevation of RNase R in response to multiple stress conditions. J. Biol. Chem. 280, 34393-34396
    • (2005) J. Biol. Chem , vol.280 , pp. 34393-34396
    • Chen, C.1    Deutscher, M.P.2
  • 14
    • 77950232101 scopus 로고    scopus 로고
    • RNase R is a highly unstable protein regulated by growth phase and stress
    • Chen, C., and Deutscher, M. P. (2010) RNase R is a highly unstable protein regulated by growth phase and stress. RNA 16, 667-672
    • (2010) RNA , vol.16 , pp. 667-672
    • Chen, C.1    Deutscher, M.P.2
  • 15
    • 77956515947 scopus 로고    scopus 로고
    • A novel mechanism for ribonuclease regulation. Transfer-messenger RNA (tmRNA) and its associated protein SmpB regulate the stability of RNase R
    • Liang, W., and Deutscher, M. P. (2010) A novel mechanism for ribonuclease regulation. Transfer-messenger RNA (tmRNA) and its associated protein SmpB regulate the stability of RNase R. J. Biol. Chem. 285, 29054-29058
    • (2010) J. Biol. Chem , vol.285 , pp. 29054-29058
    • Liang, W.1    Deutscher, M.P.2
  • 16
    • 80053595149 scopus 로고    scopus 로고
    • Acetylation regulates the stability of a bacterial protein. Growth stage-dependent modification of RNase R
    • Liang, W., Malhotra, A., and Deutscher, M. P. (2011) Acetylation regulates the stability of a bacterial protein. Growth stage-dependent modification of RNase R. Mol. Cell 44, 160-166
    • (2011) Mol. Cell , vol.44 , pp. 160-166
    • Liang, W.1    Malhotra, A.2    Deutscher, M.P.3
  • 17
    • 84866939617 scopus 로고    scopus 로고
    • Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases
    • Liang, W., and Deutscher, M. P. (2012) Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases. J. Biol. Chem. 287, 33472-33479
    • (2012) J. Biol. Chem , vol.287 , pp. 33472-33479
    • Liang, W.1    Deutscher, M.P.2
  • 18
    • 84055212205 scopus 로고    scopus 로고
    • Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)
    • Liang, W., and Deutscher, M. P. (2012) Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ). RNA 18, 37-41
    • (2012) RNA , vol.18 , pp. 37-41
    • Liang, W.1    Deutscher, M.P.2
  • 19
    • 33751358590 scopus 로고    scopus 로고
    • RNase R degrades nonstop mRNAs selectively in an SmpB-tmRNA-dependent manner
    • Richards, J., Mehta, P., and Karzai, A. W. (2006) RNase R degrades nonstop 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
  • 20
    • 78649617733 scopus 로고    scopus 로고
    • Nonstop mRNA decay initiates at the ribosome
    • Ge, Z., Mehta, P., Richards, J., and Karzai, A. W. (2010) Nonstop mRNA decay initiates at the ribosome. Mol. Microbiol. 78, 1159-1170
    • (2010) Mol. Microbiol , vol.78 , pp. 1159-1170
    • Ge, Z.1    Mehta, P.2    Richards, J.3    Karzai, A.W.4
  • 22
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and Wanner, B. L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 97, 6640-6645
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 23
    • 0029987860 scopus 로고    scopus 로고
    • 10SRNAis associated with 70 S ribosome particles in Escherichia coli
    • Komine, Y., Kitabatake, M., and Inokuchi, H. (1996) 10SRNAis associated with 70 S 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
  • 24
    • 26944431987 scopus 로고    scopus 로고
    • Ribosome rescue. tmRNA tagging activity and capacity in Escherichia coli
    • Moore, S. D., and Sauer, R. T. (2005) Ribosome rescue. tmRNA tagging activity and capacity in Escherichia coli. Mol. Microbiol. 58, 456-466
    • (2005) Mol. Microbiol , vol.58 , pp. 456-466
    • Moore, S.D.1    Sauer, R.T.2
  • 25
    • 36849093840 scopus 로고    scopus 로고
    • Functional SmpB-ribosome interactions require tmRNA
    • Sundermeier, T. R., and Karzai, A. W. (2007) Functional SmpB-ribosome interactions require tmRNA. J. Biol. Chem. 282, 34779-34786
    • (2007) J. Biol. Chem , vol.282 , pp. 34779-34786
    • Sundermeier, T.R.1    Karzai, A.W.2
  • 26
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K. C., Waller, P. R., and Sauer, R. T. (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271, 990-993
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 27
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 28
    • 61849152964 scopus 로고    scopus 로고
    • The Arabidopsis homologs of CCR4-associated factor 1 show mRNA deadenylation activity and play a role in plant defence responses
    • Liang, W., Li, C., Liu, F., Jiang, H., Li, S., Sun, J., Wu, X., and Li, C. (2009) The Arabidopsis homologs of CCR4-associated factor 1 show mRNA deadenylation activity and play a role in plant defence responses. Cell Res. 19, 307-316
    • (2009) Cell Res , vol.19 , pp. 307-316
    • Liang, W.1    Li, C.2    Liu, F.3    Jiang, H.4    Li, S.5    Sun, J.6    Wu, X.7    Li, C.8
  • 29
    • 33750378915 scopus 로고    scopus 로고
    • The genomic sequence of Wisteria vein mosaic virus and its similarities with other potyviruses
    • Liang, W. X., Song, L. M., Tian, G. Z., Li, H. F., and Fan, Z. F. (2006) The genomic sequence of Wisteria vein mosaic virus and its similarities with other potyviruses. Arch. Virol. 151, 2311-2319
    • (2006) Arch. Virol , vol.151 , pp. 2311-2319
    • Liang, W.X.1    Song, L.M.2    Tian, G.Z.3    Li, H.F.4    Fan, Z.F.5
  • 31
    • 65249190330 scopus 로고    scopus 로고
    • Initiation of ribosome degradation during starvation in Escherichia coli
    • Zundel, M. A., Basturea, G. N., and Deutscher, M. P. (2009) Initiation of ribosome degradation during starvation in Escherichia coli. RNA 15, 977-983
    • (2009) RNA , vol.15 , pp. 977-983
    • Zundel, M.A.1    Basturea, G.N.2    Deutscher, M.P.3
  • 32
    • 0017342477 scopus 로고
    • Accumulation of nucleotides by starved Escherichia coli cells as a probe for the involvement of ribonucleases in ribonucleic acid degradation
    • Cohen, L., and Kaplan, R. (1977) Accumulation of nucleotides by starved Escherichia coli cells as a probe for the involvement of ribonucleases in ribonucleic acid degradation. J. Bacteriol. 129, 651-657
    • (1977) J. Bacteriol , vol.129 , pp. 651-657
    • Cohen, L.1    Kaplan, R.2
  • 33
    • 78751468963 scopus 로고    scopus 로고
    • Degradation of ribosomal RNA during starvation. Comparison to quality control during steady-state growth and a role for RNase PH
    • Basturea, G. N., Zundel, M. A., and Deutscher, M. P. (2011) Degradation of ribosomal RNA during starvation. Comparison to quality control during steady-state growth and a role for RNase PH. RNA 17, 338-345
    • (2011) RNA , vol.17 , pp. 338-345
    • Basturea, G.N.1    Zundel, M.A.2    Deutscher, M.P.3
  • 35
    • 79955008757 scopus 로고    scopus 로고
    • Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways
    • Chadani, Y., Ono, K., Kutsukake, K., and Abo, T. (2011) Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways. Mol. Microbiol. 80, 772-785
    • (2011) Mol. Microbiol , vol.80 , pp. 772-785
    • Chadani, Y.1    Ono, K.2    Kutsukake, K.3    Abo, T.4
  • 36
    • 84877142636 scopus 로고    scopus 로고
    • Multiple exoribonucleases catalyze maturation of the 3' terminus of 16S ribosomal RNA (rRNA)
    • Sulthana, S., and Deutscher, M. P. (2013) Multiple exoribonucleases catalyze maturation of the 3' terminus of 16S ribosomal RNA (rRNA). J. Biol. Chem. 288, 12574-12579
    • (2013) J. Biol. Chem , vol.288 , pp. 12574-12579
    • Sulthana, S.1    Deutscher, M.P.2


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