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Volumn 88, Issue 2, 2006, Pages 151-161

Analysis of the Escherichia coli RNA degradosome composition by a proteomic approach

Author keywords

DnaK; Mass spectrometry; Polynucleotide phosphorylase; Ribonuclease E; RNA degradation

Indexed keywords

BACTERIAL RNA; CHAPERONE; RIBONUCLEASE;

EID: 27944504787     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.07.012     Document Type: Article
Times cited : (63)

References (46)
  • 2
    • 0028269435 scopus 로고
    • Copurification of E. coli RNase e and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation
    • A.J. Carpousis, G. Van Houwe, C. Ehretsmann, and H.M. Krisch Copurification of E. coli RNase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation Cell 76 1994 889 900
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 3
    • 0027945686 scopus 로고
    • A protein complex mediating mRNA degradation in Escherichia coli
    • B. Py, H. Causton, E.A. Mudd, and C.F. Higgins A protein complex mediating mRNA degradation in Escherichia coli Mol. Microbiol. 14 1994 717 729
    • (1994) Mol. Microbiol. , vol.14 , pp. 717-729
    • Py, B.1    Causton, H.2    Mudd, E.A.3    Higgins, C.F.4
  • 4
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • B. Py, C.F. Higgins, H.M. Krisch, and A.J. Carpousis A DEAD-box RNA helicase in the Escherichia coli RNA degradosome Nature 381 1996 169 172
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 6
    • 0036549769 scopus 로고    scopus 로고
    • The Escherichia coli RNA degradosome: Structure, function and relationship in other ribonucleolytic multienzyme complexes
    • A.J. Carpousis The Escherichia coli RNA degradosome: structure, function and relationship in other ribonucleolytic multienzyme complexes Biochem. Soc. Trans. 30 2002 150 155
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 150-155
    • Carpousis, A.J.1
  • 7
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • R. Raijmakers, G. Schilders, and G.J. Pruijn The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm Eur. J. Cell Biol. 83 2004 175 183
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.J.3
  • 9
    • 0032578486 scopus 로고    scopus 로고
    • The endoribonucleolytic N-terminal half of Escherichia coli RNase e is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly
    • V.R. Kaberdin, A. Miczak, J.S. Jakobsen, S. Lin-Chao, K.J. McDowall, and A. von Gabain The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly Proc. Natl. Acad. Sci. USA 95 1998 11637 11642
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11637-11642
    • Kaberdin, V.R.1    Miczak, A.2    Jakobsen, J.S.3    Lin-Chao, S.4    McDowall, K.J.5    Von Gabain, A.6
  • 11
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEAD-box RNA helicase
    • G.A. Coburn, X. Miao, D.J. Briant, and G.A. Mackie Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEAD-box RNA helicase Genes Dev. 13 1999 2594 2603
    • (1999) Genes Dev. , vol.13 , pp. 2594-2603
    • Coburn, G.A.1    Miao, X.2    Briant, D.J.3    MacKie, G.A.4
  • 12
    • 8544261105 scopus 로고    scopus 로고
    • Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli
    • T. Morita, H. Kawamoto, T. Mizota, T. Inada, and H. Aiba Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli Mol. Microbiol. 54 2004 1063 1075
    • (2004) Mol. Microbiol. , vol.54 , pp. 1063-1075
    • Morita, T.1    Kawamoto, H.2    Mizota, T.3    Inada, T.4    Aiba, H.5
  • 13
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • E. Blum, B. Py, A.J. Carpousis, and C.F. Higgins Polyphosphate kinase is a component of the Escherichia coli RNA degradosome Mol. Microbiol. 26 1997 387 398
    • (1997) Mol. Microbiol. , vol.26 , pp. 387-398
    • Blum, E.1    Py, B.2    Carpousis, A.J.3    Higgins, C.F.4
  • 14
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase e in a multicomponent ribonucleolytic complex
    • A. Miczak, V.R. Kaberdin, C.L. Wei, and S. Lin-Chao Proteins associated with RNase E in a multicomponent ribonucleolytic complex Proc. Natl. Acad. Sci. USA 93 1996 3865 3869
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 15
    • 9644284618 scopus 로고    scopus 로고
    • Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: Evidence for a 'cold shock degradosome'
    • A. Prud'homme-Ǵńreux, R.K. Beran, I. Iost, C.S. Ramey, G.A. Mackie, and R.W. Simons Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome' Mol. Microbiol. 54 2004 1409 1421
    • (2004) Mol. Microbiol. , vol.54 , pp. 1409-1421
    • Prud'Homme-Ǵńreux, A.1    Beran, R.K.2    Iost, I.3    Ramey, C.S.4    MacKie, G.A.5    Simons, R.W.6
  • 16
    • 9644277144 scopus 로고    scopus 로고
    • The RNase e of Escherichia coli has at least two binding sites for DEAD-box RNA helicases: Functional replacement of RhlB by RhlE
    • V. Khemici, I. Toesca, L. Poljak, N.F. Vanzo, and A.J. Carpousis The RNase E of Escherichia coli has at least two binding sites for DEAD-box RNA helicases: functional replacement of RhlB by RhlE Mol. Microbiol. 54 2004 1422 1430
    • (2004) Mol. Microbiol. , vol.54 , pp. 1422-1430
    • Khemici, V.1    Toesca, I.2    Poljak, L.3    Vanzo, N.F.4    Carpousis, A.J.5
  • 17
    • 0032970686 scopus 로고    scopus 로고
    • Poly(A) polymerase I of Escherichia coli: Characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation
    • L.C. Raynal, and A.J. Carpousis Poly(A) polymerase I of Escherichia coli: characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation Mol. Microbiol. 32 1999 765 775
    • (1999) Mol. Microbiol. , vol.32 , pp. 765-775
    • Raynal, L.C.1    Carpousis, A.J.2
  • 18
    • 0035943737 scopus 로고    scopus 로고
    • Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase e
    • Y. Feng, H. Huang, J. Liao, and S.N. Cohen Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E J. Biol. Chem. 276 2001 31651 31656
    • (2001) J. Biol. Chem. , vol.276 , pp. 31651-31656
    • Feng, Y.1    Huang, H.2    Liao, J.3    Cohen, S.N.4
  • 19
    • 0035824631 scopus 로고    scopus 로고
    • Advances in proteome analysis by mass spectrometry
    • T.J. Griffin, and R. Aebersold Advances in proteome analysis by mass spectrometry J. Biol. Chem. 276 2001 45497 45500
    • (2001) J. Biol. Chem. , vol.276 , pp. 45497-45500
    • Griffin, T.J.1    Aebersold, R.2
  • 20
  • 21
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • S.P. Gygi, B. Rist, S.A. Gerber, F. Turecek, M.H. Gelb, and R. Aebersold Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 17 1999 994 999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 22
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • D.A. Wolters, M.P. Washburn, and J.R. Yates III An automated multidimensional protein identification technology for shotgun proteomics Anal. Chem. 73 2001 5683 5690
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 23
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • K.A. Datsenko, and B.L. Wanner One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc. Natl. Acad. Sci. USA 97 2000 6640 6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 24
    • 0025048776 scopus 로고
    • Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
    • B. Bukau, and G.C. Walker Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone EMBO J. 9 1990 4027 4036
    • (1990) EMBO J. , vol.9 , pp. 4027-4036
    • Bukau, B.1    Walker, G.C.2
  • 25
    • 0013797789 scopus 로고
    • Growth abnormalities in Hfr derivatives of Escherichia coli strain C
    • I. Sasaki, and G. Bertani Growth abnormalities in Hfr derivatives of Escherichia coli strain C J. Gen. Microbiol. 40 1965 365 376
    • (1965) J. Gen. Microbiol. , vol.40 , pp. 365-376
    • Sasaki, I.1    Bertani, G.2
  • 26
    • 0029787968 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase of Escherichia coli is required for the establishment of bacteriophage P4 immunity
    • F. Piazza, M. Zappone, M. Sana, F. Briani, and G. Dehò Polynucleotide phosphorylase of Escherichia coli is required for the establishment of bacteriophage P4 immunity J. Bacteriol. 178 1996 5513 5521
    • (1996) J. Bacteriol. , vol.178 , pp. 5513-5521
    • Piazza, F.1    Zappone, M.2    Sana, M.3    Briani, F.4    Dehò, G.5
  • 28
    • 2342625898 scopus 로고    scopus 로고
    • A mutation in polynucleotide phosphorylase from Escherichia coli impairing RNA binding and degradosome stability
    • M.E. Regonesi, F. Briani, A. Ghetta, S. Zangrossi, D. Ghisotti, P. Tortora, and G. Dehò A mutation in polynucleotide phosphorylase from Escherichia coli impairing RNA binding and degradosome stability Nucleic Acids Res. 32 2004 1006 1017
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1006-1017
    • Regonesi, M.E.1    Briani, F.2    Ghetta, A.3    Zangrossi, S.4    Ghisotti, D.5    Tortora, P.6    Dehò, G.7
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0002725941 scopus 로고    scopus 로고
    • Multidimensional protein identification technology as an effective tool for proteomics
    • D. Lin, A. Alpert, and J.3. Yates Multidimensional protein identification technology as an effective tool for proteomics Am.Genomic/Proteomic Technol. 1 2001 38 46
    • (2001) Am.Genomic/Proteomic Technol. 1 , pp. 38-46
    • Lin, D.1    Alpert, A.2    Yates III, J.3
  • 34
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • J. Eng, A. McCormack, and J. Yates An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database J. Am. Soc. Mass Spectrom. 5 1994 976 989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.2    Yates, J.3
  • 36
    • 21744435256 scopus 로고    scopus 로고
    • Identification of proteins released by pancreatic cancer cells by multidimensional protein identification technology: A strategy for identification of novel cancer markers
    • P. Mauri, A. Scarpa, A.C. Nascimbeni, L. Benazzi, E. Parmagnani, A. Mafficini, M. Della Peruta, C. Bassi, K. Miyazaki, and C. Sorio Identification of proteins released by pancreatic cancer cells by multidimensional protein identification technology: a strategy for identification of novel cancer markers FASEB J. 19 2005 1125 1127
    • (2005) FASEB J. , vol.19 , pp. 1125-1127
    • Mauri, P.1    Scarpa, A.2    Nascimbeni, A.C.3    Benazzi, L.4    Parmagnani, E.5    Mafficini, A.6    Della Peruta, M.7    Bassi, C.8    Miyazaki, K.9    Sorio, C.10
  • 37
    • 0014806605 scopus 로고
    • Kinetics of polymerization and phosphorolysis reactions of Escherichia coli polynucleotide phosphorylase. Evidence for multiple binding of polynucleotide in phosphorolysis
    • T. Godefroy Kinetics of polymerization and phosphorolysis reactions of Escherichia coli polynucleotide phosphorylase. Evidence for multiple binding of polynucleotide in phosphorolysis Eur. J. Biochem. 14 1970 222 231
    • (1970) Eur. J. Biochem. , vol.14 , pp. 222-231
    • Godefroy, T.1
  • 38
    • 0017648969 scopus 로고
    • Purification and characterization of polynucleotide phosphorylase from Escherichia coli. Probe for the analysis of 3′ sequences of RNA
    • H. Soreq, and U.Z. Littauer Purification and characterization of polynucleotide phosphorylase from Escherichia coli. Probe for the analysis of 3′ sequences of RNA J. Biol. Chem. 252 1977 6885 6888
    • (1977) J. Biol. Chem. , vol.252 , pp. 6885-6888
    • Soreq, H.1    Littauer, U.Z.2
  • 39
    • 0016421634 scopus 로고
    • Enolase from Escherichia coli
    • T.G. Spring, and F. Wold Enolase from Escherichia coli Methods Enzymol. 42 1975 323 329
    • (1975) Methods Enzymol. , vol.42 , pp. 323-329
    • Spring, T.G.1    Wold, F.2
  • 40
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • H. Liu, R.G. Sadygov, and J.R. Yates III A model for random sampling and estimation of relative protein abundance in shotgun proteomics Anal. Chem. 76 2004 4193 4201
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 42
    • 0027250040 scopus 로고
    • Escherichia coli endoribonuclease RNase E: Autoregulation of expression and site-specific cleavage of mRNA
    • E.A. Mudd, and C.F. Higgins Escherichia coli endoribonuclease RNase E: autoregulation of expression and site-specific cleavage of mRNA Mol. Microbiol. 9 1993 557 568
    • (1993) Mol. Microbiol. , vol.9 , pp. 557-568
    • Mudd, E.A.1    Higgins, C.F.2
  • 43
    • 0028797303 scopus 로고
    • RNase e autoregulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: Unusual sensitivity of the rne transcript to RNase e activity
    • C. Jain, and J.G. Belasco RNase E autoregulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: unusual sensitivity of the rne transcript to RNase E activity Genes Dev. 9 1995 84 96
    • (1995) Genes Dev. , vol.9 , pp. 84-96
    • Jain, C.1    Belasco, J.G.2
  • 44
    • 0029438136 scopus 로고
    • Autoregulation of RNase e synthesis in Escherichia coli
    • C. Jain, and J.G. Belasco Autoregulation of RNase E synthesis in Escherichia coli Nucleic Acids Symp. Ser. 1995 85 88
    • (1995) Nucleic Acids Symp. Ser. , pp. 85-88
    • Jain, C.1    Belasco, J.G.2
  • 45
    • 0036197752 scopus 로고    scopus 로고
    • RNase e levels in Escherichia coli are controlled by a complex regulatory system that involves transcription of the rne gene from three promoters
    • M.C. Ow, Q. Liu, B.K. Mohanty, M.E. Andrew, V.F. Maples, and S.R. Kushner RNase E levels in Escherichia coli are controlled by a complex regulatory system that involves transcription of the rne gene from three promoters Mol. Microbiol. 43 2002 159 171
    • (2002) Mol. Microbiol. , vol.43 , pp. 159-171
    • Ow, M.C.1    Liu, Q.2    Mohanty, B.K.3    Andrew, M.E.4    Maples, V.F.5    Kushner, S.R.6
  • 46
    • 0029889965 scopus 로고    scopus 로고
    • RNase e polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
    • M. Kido, K. Yamanaka, T. Mitani, H. Niki, T. Ogura, and S. Hiraga RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli J. Bacteriol. 178 1996 3917 3925
    • (1996) J. Bacteriol. , vol.178 , pp. 3917-3925
    • Kido, M.1    Yamanaka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6


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