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Volumn 1794, Issue 8, 2009, Pages 1107-1114

Identification and functional analysis of RNase E of Vibrio angustum S14 and two-hybrid analysis of its interaction partners

Author keywords

Bacterial Adenylate Cyclase two hybrid (BACTH); Degradosome; Enolase; Microdomain; PNPase; RNase E

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; UNCLASSIFIED DRUG; VIBRIO ANGUSTUM RIBONUCLEASE E;

EID: 67349116514     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.03.016     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 0037162469 scopus 로고    scopus 로고
    • Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays
    • Bernstein J.A., Khodursky A.B., Lin P.H., Lin-Chao S., and Cohen S.N. Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9697-9702
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9697-9702
    • Bernstein, J.A.1    Khodursky, A.B.2    Lin, P.H.3    Lin-Chao, S.4    Cohen, S.N.5
  • 2
    • 0033368475 scopus 로고    scopus 로고
    • Messenger RNA stability and its role in control of gene expression in bacteria and phages
    • Grunberg-Manago M. Messenger RNA stability and its role in control of gene expression in bacteria and phages. Annu. Rev. Genet. 33 (1999) 193-227
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 3
    • 0023663908 scopus 로고
    • Differential messenger-RNA stability controls relative gene-expression within a polycistronic operon
    • Newbury S.F., Smith N.H., and Higgins C.F. Differential messenger-RNA stability controls relative gene-expression within a polycistronic operon. Cell 51 (1987) 1131-1143
    • (1987) Cell , vol.51 , pp. 1131-1143
    • Newbury, S.F.1    Smith, N.H.2    Higgins, C.F.3
  • 4
    • 0033577789 scopus 로고    scopus 로고
    • RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA
    • Li Z., Pandit S., and Deutscher M.P. RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA. EMBO J. 18 (1999) 2878-2885
    • (1999) EMBO J. , vol.18 , pp. 2878-2885
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 5
    • 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., and Lin Y.T. RNase E is required for the maturation of SsrA RNA and normal SsrA RNA peptide-tagging activity. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12406-12411
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12406-12411
    • Lin-Chao, S.1    Wei, C.L.2    Lin, Y.T.3
  • 6
    • 0036274640 scopus 로고    scopus 로고
    • RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli
    • Lee K., Bernstein J.A., and Cohen S.N. RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli. Mol. Microbiol. 43 (2002) 1445-1456
    • (2002) Mol. Microbiol. , vol.43 , pp. 1445-1456
    • Lee, K.1    Bernstein, J.A.2    Cohen, S.N.3
  • 7
    • 0036571060 scopus 로고    scopus 로고
    • Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli
    • Ow M.C., and Kushner S.R. Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli. Genes Dev. 16 (2002) 1102-1115
    • (2002) Genes Dev. , vol.16 , pp. 1102-1115
    • Ow, M.C.1    Kushner, S.R.2
  • 8
    • 0017887243 scopus 로고
    • Conditional lethal mutant of Escherichia coli which affects processing of ribosomal RNA
    • Apirion D., and Lassar A.B. Conditional lethal mutant of Escherichia coli which affects processing of ribosomal RNA. J. Biol. Chem. 253 (1978) 1738-1742
    • (1978) J. Biol. Chem. , vol.253 , pp. 1738-1742
    • Apirion, D.1    Lassar, A.B.2
  • 9
    • 0018791193 scopus 로고
    • Conditional lethal mutation in an Escherichia coli strain with a longer chemical lifetime of mRNA
    • Ono M., and Kuwano M. Conditional lethal mutation in an Escherichia coli strain with a longer chemical lifetime of mRNA. J. Mol. Biol. 129 (1979) 343-357
    • (1979) J. Mol. Biol. , vol.129 , pp. 343-357
    • Ono, M.1    Kuwano, M.2
  • 10
    • 0028269435 scopus 로고
    • Copurification of Escherichia coli RNase E and PNPase - evidence for a specific association between 2 enzymes important in RNA processing and degradation
    • Carpousis A.J., Vanhouwe G., Ehretsmann C., and Krisch H.M. Copurification of Escherichia coli RNase E and PNPase - evidence for a specific association between 2 enzymes important in RNA processing and degradation. Cell 76 (1994) 889-900
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Vanhouwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 11
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • Condon C., and Putzer H. The phylogenetic distribution of bacterial ribonucleases. Nucleic Acids Res. 30 (2002) 5339-5346
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 12
    • 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
    • Ow M.C., Liu Q., Mohanty B.K., Andrew M.E., Maples F., and Kushner S.R. 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, F.5    Kushner, S.R.6
  • 13
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEAD-box RNA helicase
    • Coburn G.A., Miao X., Briant D.J., and Mackie G.A. 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
  • 14
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou G.-G., Chang H.-Y., Lin C.-S., and Lin-Chao S. DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J. Biol. Chem. 277 (2002) 41157-41162
    • (2002) J. Biol. Chem. , vol.277 , pp. 41157-41162
    • Liou, G.-G.1    Chang, H.-Y.2    Lin, C.-S.3    Lin-Chao, S.4
  • 15
    • 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
    • Kaberdin R., Miczak A., Jakobsen J.S., Lin-Chao S., McDowall K.J., and von Gabain A. 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. U. S. A. 95 (1998) 11637-11642
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11637-11642
    • Kaberdin, R.1    Miczak, A.2    Jakobsen, J.S.3    Lin-Chao, S.4    McDowall, K.J.5    von Gabain, A.6
  • 17
    • 0036549769 scopus 로고    scopus 로고
    • The Escherichia coli RNA degradosome: structure, function and relationship to other ribonucleolytic multienyzme complexes
    • Carpousis A.J. The Escherichia coli RNA degradosome: structure, function and relationship to other ribonucleolytic multienyzme complexes. Biochem. Soc. Trans. 30 (2002) 150-155
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 150-155
    • Carpousis, A.J.1
  • 18
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • Miczak A., Kaaberdin R., Wei C.L., and Linchao S. Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 3865-3869
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaaberdin, R.2    Wei, C.L.3    Linchao, S.4
  • 19
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py B., Higgins C.F., Krisch H.M., and Carpousis A.J. 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
  • 21
    • 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'
    • Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A., and Simons R.W. 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-Genereux, A.1    Beran, R.K.2    Iost, I.3    Ramey, C.S.4    Mackie, G.A.5    Simons, R.W.6
  • 22
    • 3242763145 scopus 로고    scopus 로고
    • Composition and activity of the Rhodobacter capsulatus degradosome vary under different oxygen concentrations
    • Jager S., Hebermehl M., Schiltz E., and Klug G. Composition and activity of the Rhodobacter capsulatus degradosome vary under different oxygen concentrations. J. Mol. Microbiol. Biotechnol. 7 (2004) 148-154
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 148-154
    • Jager, S.1    Hebermehl, M.2    Schiltz, E.3    Klug, G.4
  • 24
    • 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
    • Morita T., Kawamoto H., Mizota T., Inada T., and Aiba H. 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
  • 25
    • 33645097025 scopus 로고    scopus 로고
    • Recognition of enolase in the Escherichia coli RNA degradosome
    • Chandran V., and Luisi B.F. Recognition of enolase in the Escherichia coli RNA degradosome. J. Mol. Biol. 358 (2006) 8-15
    • (2006) J. Mol. Biol. , vol.358 , pp. 8-15
    • Chandran, V.1    Luisi, B.F.2
  • 26
    • 0002640352 scopus 로고
    • Responses of marine bacteria under starvation conditions at a solid-water interphase.
    • Humphrey B., Kjelleberg S., and Marshall K.C. Responses of marine bacteria under starvation conditions at a solid-water interphase. Appl. Environ. Microbiol. 45 (1983) 43-47
    • (1983) Appl. Environ. Microbiol. , vol.45 , pp. 43-47
    • Humphrey, B.1    Kjelleberg, S.2    Marshall, K.C.3
  • 27
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero P., Obradovic Z., and Dunker A.K. Sequence data analysis for long disordered regions prediction in the calcineurin family. Genome Informatics 8 (1997) 110-124
    • (1997) Genome Informatics , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 34
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: exploring protein sequences for globularity and disorder
    • Linding R., Russell R.B., Neduva V., and Gibson T.J. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res. 31 (2003) 3701-3708
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 35
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Vandyke M., and Stock J. Predicting coiled coils from protein sequences. Science 252 (1991) 1162-1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Vandyke, M.2    Stock, J.3
  • 36
    • 0033532514 scopus 로고    scopus 로고
    • Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA
    • Wachi M., Umitsuki G., Shimizu M., Takada A., and Nagai K. Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA. Biochem. Biophys. Res. Commun. 259 (1999) 483-488
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 483-488
    • Wachi, M.1    Umitsuki, G.2    Shimizu, M.3    Takada, A.4    Nagai, K.5
  • 37
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova G., Pidoux J., Ullmann A., and Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5752-5756
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 39
    • 54249138245 scopus 로고    scopus 로고
    • The RNase E of Escherichia coli is a membrane-binding protein
    • Khemici V., Poljak L., Luisi B.F., and Carpousis A.J. The RNase E of Escherichia coli is a membrane-binding protein. Mol. Microbiol. 70 (2008) 799-813
    • (2008) Mol. Microbiol. , vol.70 , pp. 799-813
    • Khemici, V.1    Poljak, L.2    Luisi, B.F.3    Carpousis, A.J.4
  • 40
    • 0023813422 scopus 로고
    • Purification and characterization of enolase from Escherichia coli
    • Dannelly H.K., and Reeves H.C. Purification and characterization of enolase from Escherichia coli. Curr. Microbiol. 17 (1988) 265-268
    • (1988) Curr. Microbiol. , vol.17 , pp. 265-268
    • Dannelly, H.K.1    Reeves, H.C.2
  • 41
    • 0015240433 scopus 로고
    • The purification and characterization of Escherichia coli enolase
    • Spring T.G., and Wold F. The purification and characterization of Escherichia coli enolase. J. Biol. Chem. 246 (1971) 6797-6802
    • (1971) J. Biol. Chem. , vol.246 , pp. 6797-6802
    • Spring, T.G.1    Wold, F.2
  • 42
    • 0025688893 scopus 로고
    • RNase E, an Endoribonuclease, has a general role in the chemical decay of Escherichia coli messenger RNA - evidence that rne and ams are the same genetic-locus
    • Mudd E.A., Krisch H.M., and Higgins C.F. RNase E, an Endoribonuclease, has a general role in the chemical decay of Escherichia coli messenger RNA - evidence that rne and ams are the same genetic-locus. Mol. Microbiol. 4 (1990) 2127-2135
    • (1990) Mol. Microbiol. , vol.4 , pp. 2127-2135
    • Mudd, E.A.1    Krisch, H.M.2    Higgins, C.F.3
  • 43
    • 33847081239 scopus 로고    scopus 로고
    • Role of intrinsic disorder in transient interactions of hub proteins
    • Singh G.P., Ganapathi M., and Dash D. Role of intrinsic disorder in transient interactions of hub proteins. Proteins-Struct. Funct. Bioinform. 66 (2007) 761-765
    • (2007) Proteins-Struct. Funct. Bioinform. , vol.66 , pp. 761-765
    • Singh, G.P.1    Ganapathi, M.2    Dash, D.3
  • 45
    • 0035176037 scopus 로고    scopus 로고
    • Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation
    • Beran R.K., and Simons R.W. Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation. Mol. Microbiol. 39 (2001) 112-125
    • (2001) Mol. Microbiol. , vol.39 , pp. 112-125
    • Beran, R.K.1    Simons, R.W.2
  • 46
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • Morita T., Maki K., and Aiba H. RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes Dev. 19 (2005) 2176-2186
    • (2005) Genes Dev. , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 47
    • 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
    • Khemici V., Toesca I., Poljak L., Vanzo N.F., and Carpousis A.J. 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


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