메뉴 건너뛰기




Volumn 18, Issue 1, 2012, Pages 37-41

Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)

Author keywords

Escherichia coli; Post translational modification; Protein stability; Ribonuclease

Indexed keywords

ENZYME; PROTEIN LYSINE ACETYLTRANSFERASE; RIBONUCLEASE; RIBONUCLEASE R; UNCLASSIFIED DRUG;

EID: 84055212205     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.030213.111     Document Type: Article
Times cited : (48)

References (22)
  • 1
    • 33644841796 scopus 로고    scopus 로고
    • RNase R affects gene expression in stationary phase: Regulation of ompA
    • Andrade JM, Cairrão F, Arraiano CM. 2006. RNase R affects gene expression in stationary phase: Regulation of ompA. Mol Microbiol 60: 219-228.
    • (2006) Mol Microbiol , vol.60 , pp. 219-228
    • Andrade, J.M.1    Cairrão, F.2    Arraiano, C.M.3
  • 3
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • DOI 10.1146/annurev.biochem.73.011303.073651
    • Blander G, Guarente L. 2004. The Sir2 family of protein deacetylases. Annu Rev Biochem 73: 417-435. (Pubitemid 39050375)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 4
    • 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 CM. 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
  • 5
    • 27144467868 scopus 로고    scopus 로고
    • Elevation of RNase R in response to multiple stress conditions
    • DOI 10.1074/jbc.C500333200
    • Chen C, Deutscher MP. 2005. Elevation of RNase R in response to multiple stress conditions. J Biol Chem 280: 34393-34396. (Pubitemid 41504566)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.41 , pp. 34393-34396
    • Chen, C.1    Deutscher, M.P.2
  • 6
    • 77950232101 scopus 로고    scopus 로고
    • RNase R is a highly unstable protein regulated by growth phase and stress
    • Chen C, Deutscher MP. 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
  • 7
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • DOI 10.1074/jbc.M202942200
    • Cheng ZF, Deutscher MP. 2002. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J Biol Chem 277: 21624-21629. (Pubitemid 34952311)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21624-21629
    • Cheng, Z.-F.1    Deutscher, M.P.2
  • 8
    • 12344330602 scopus 로고    scopus 로고
    • An important role for RNase R in mRNA decay
    • DOI 10.1016/j.molcel.2004.11.048, PII S1097276504007701
    • Cheng ZF, Deutscher MP. 2005. An important role for RNase R in mRNA decay. Mol Cell 17: 313-318. (Pubitemid 40138624)
    • (2005) Molecular Cell , vol.17 , Issue.2 , pp. 313-318
    • Cheng, Z.-F.1    Deutscher, M.P.2
  • 9
    • 0032486392 scopus 로고    scopus 로고
    • The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R
    • DOI 10.1074/jbc.273.23.14077
    • Cheng ZF, Zuo Y, Li Z, Rudd KE, Deutscher MP. 1998. The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J Biol Chem 273: 14077-14080. (Pubitemid 28319112)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.23 , pp. 14077-14080
    • Cheng, Z.-F.1    Zuo, Y.2    Li, Z.3    Rudd, K.E.4    Deutscher, M.P.5
  • 10
    • 0029065955 scopus 로고
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158: 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wachernagel, W.2
  • 12
    • 79952910566 scopus 로고    scopus 로고
    • ε-lysine acetylation control conserved in all three life domains
    • ε-lysine acetylation control conserved in all three life domains. Microbe 5: 340-344.
    • (2010) Microbe , vol.5 , pp. 340-344
    • Escalante-Semerena, J.C.1
  • 13
    • 77954013335 scopus 로고    scopus 로고
    • Bacterial protein acetylation: The dawning of a new age
    • Hu LI, Lima BP, Wolfe AJ. 2010. Bacterial protein acetylation: The dawning of a new age. Mol Microbiol 77: 15-21.
    • (2010) Mol Microbiol , vol.77 , pp. 15-21
    • Hu, L.I.1    Lima, B.P.2    Wolfe, A.J.3
  • 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, Deutscher MP. 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 17: 29054-29058.
    • (2010) J Biol Chem , vol.17 , pp. 29054-29058
    • Liang, W.1    Deutscher, M.P.2
  • 16
    • 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, 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
  • 17
    • 80053595149 scopus 로고    scopus 로고
    • Acetylation regulates the stability of a bacterial protein: Growth stage-dependent modification of RNase R
    • Liang W, Malhotra A, Deutscher MP. 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
  • 18
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • DOI 10.1074/jbc.M606744200
    • Vincent HA, Deutscher MP. 2006. Substrate recognition and catalysis by the exoribonuclease RNase R. J Biol Chem 281: 29769-29775. (Pubitemid 44536986)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 19
    • 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 HA, Deutscher MP. 2009a. 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
  • 20
    • 62049085767 scopus 로고    scopus 로고
    • Insights into how RNase R degrades structured RNA: Analysis of the nuclease domain
    • Vincent HA, Deutscher MP. 2009b. 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
  • 21
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, Yao J, Li H, Xie L, Zhao W, Yao Y, et al. 2010. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6    Li, H.7    Xie, L.8    Zhao, W.9    Yao, Y.10
  • 22
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo Y, Deutscher MP. 2001. Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution. Nucleic Acids Res 29: 1017-1026. (Pubitemid 32186186)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.