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Volumn 76, Issue 2, 2010, Pages 286-301

Functional regions of the N-terminal domain of the antiterminator RfaH

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; PROTEIN RFAH; RNA POLYMERASE; UNCLASSIFIED DRUG; BACTERIAL DNA; DNA DIRECTED RNA POLYMERASE; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING; RFAH PROTEIN, E COLI; TRANSACTIVATOR PROTEIN;

EID: 77951157212     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07056.x     Document Type: Article
Times cited : (55)

References (42)
  • 1
    • 0034691146 scopus 로고    scopus 로고
    • Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
    • Artsimovitch, I. Landick, R. (2000) Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc Natl Acad Sci USA 97 : 7090 7095.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7090-7095
    • Artsimovitch, I.1    Landick, R.2
  • 2
    • 0037133970 scopus 로고    scopus 로고
    • RfaH stimulates chain elongation by bacterial transcription complexes after recruitment by the exposed nontemplate DNA strand
    • Artsimovitch, I. Landick, R. (2002) RfaH stimulates chain elongation by bacterial transcription complexes after recruitment by the exposed nontemplate DNA strand. Cell 109 : 193 203.
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 3
    • 0030718529 scopus 로고    scopus 로고
    • RfaH and the ops element, components of a novel system controlling bacterial transcription elongation
    • Bailey, M.J., Hughes, C. Koronakis, V. (1997) RfaH and the ops element, components of a novel system controlling bacterial transcription elongation. Mol Microbiol 26 : 845 851. (Pubitemid 27507870)
    • (1997) Molecular Microbiology , vol.26 , Issue.5 , pp. 845-851
    • Bailey, M.J.A.1    Hughes, C.2    Koronakis, V.3
  • 4
    • 0033956695 scopus 로고    scopus 로고
    • In vitro recruitment of the RfaH regulatory protein into a specialised transcription complex, directed by the nucleic acid ops element
    • Bailey, M.J., Hughes, C. Koronakis, V. (2000) In vitro recruitment of the RfaH regulatory protein into a specialised transcription complex, directed by the nucleic acid ops element. Mol Gen Genet 262 : 1052 1059. (Pubitemid 30072134)
    • (2000) Molecular and General Genetics , vol.262 , Issue.6 , pp. 1052-1059
    • Bailey, M.J.A.1    Hughes, C.2    Koronakis, V.3
  • 5
    • 0026609257 scopus 로고
    • Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes
    • Bailey, M.J., Koronakis, V., Schmoll, T. Hughes, C. (1992) Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes. Mol Microbiol 6 : 1003 1012.
    • (1992) Mol Microbiol , vol.6 , pp. 1003-1012
    • Bailey, M.J.1    Koronakis, V.2    Schmoll, T.3    Hughes, C.4
  • 7
    • 34147155174 scopus 로고    scopus 로고
    • Structural Basis for Converting a General Transcription Factor into an Operon-Specific Virulence Regulator
    • DOI 10.1016/j.molcel.2007.02.021, PII S1097276507001219
    • Belogurov, G.A., Vassylyeva, M.N., Svetlov, V., Klyuyev, S., Grishin, N.V., Vassylyev, D.G. Artsimovitch, I. (2007) Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Mol Cell 26 : 117 129. (Pubitemid 46553793)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 117-129
    • Belogurov, G.A.1    Vassylyeva, M.N.2    Svetlov, V.3    Klyuyev, S.4    Grishin, N.V.5    Vassylyev, DmitryG.6    Artsimovitch, I.7
  • 9
    • 67349099134 scopus 로고    scopus 로고
    • RNA-directed DNA methylation requires an AGO4-interacting member of the SPT5 elongation factor family
    • Bies-Etheve, N., Pontier, D., Lahmy, S., Picart, C., Vega, D., Cooke, R. Lagrange, T. (2009) RNA-directed DNA methylation requires an AGO4-interacting member of the SPT5 elongation factor family. EMBO Rep 10 : 649 654.
    • (2009) EMBO Rep , vol.10 , pp. 649-654
    • Bies-Etheve, N.1    Pontier, D.2    Lahmy, S.3    Picart, C.4    Vega, D.5    Cooke, R.6    Lagrange, T.7
  • 10
    • 0029002685 scopus 로고
    • NusG is required to overcome a kinetic limitation to Rho function at an intragenic terminator
    • Burns, C.M. Richardson, J.P. (1995) NusG is required to overcome a kinetic limitation to Rho function at an intragenic terminator. Proc Natl Acad Sci USA 92 : 4738 4742.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4738-4742
    • Burns, C.M.1    Richardson, J.P.2
  • 11
    • 44249091644 scopus 로고    scopus 로고
    • Termination factor Rho and its cofactors NusA and NusG silence foreign DNA in E. coli
    • DOI 10.1126/science.1152763
    • Cardinale, C.J., Washburn, R.S., Tadigotla, V.R., Brown, L.M., Gottesman, M.E. Nudler, E. (2008) Termination factor Rho and its cofactors NusA and NusG silence foreign DNA in E. coli. Science 320 : 935 938. (Pubitemid 351929589)
    • (2008) Science , vol.320 , Issue.5878 , pp. 935-938
    • Cardinale, C.J.1    Washburn, R.S.2    Tadigotla, V.R.3    Brown, L.M.4    Gottesman, M.E.5    Nudler, E.6
  • 12
    • 1942539312 scopus 로고    scopus 로고
    • Highly Divergent RfaH Orthologs from Pathogenic Proteobacteria Can Substitute for Escherichia coli RfaH both In Vivo and In Vitro
    • DOI 10.1128/JB.186.9.2829-2840.2004
    • Carter, H.D., Svetlov, V. Artsimovitch, I. (2004) Highly divergent RfaH orthologs from pathogenic proteobacteria can substitute for Escherichia coli RfaH both in vivo and in vitro. J Bacteriol 186 : 2829 2840. (Pubitemid 38525938)
    • (2004) Journal of Bacteriology , vol.186 , Issue.9 , pp. 2829-2840
    • Carter, H.D.1    Svetlov, V.2    Artsimovitch, I.3
  • 13
    • 0033579380 scopus 로고    scopus 로고
    • Structure of a transcribing T7 RNA polymerase initiation complex
    • DOI 10.1126/science.286.5448.2305
    • Cheetham, G.M. Steitz, T.A. (1999) Structure of a transcribing T7 RNA polymerase initiation complex. Science 286 : 2305 2309. (Pubitemid 30016883)
    • (1999) Science , vol.286 , Issue.5448 , pp. 2305-2309
    • Cheetham, G.M.T.1    Steitz, T.A.2
  • 14
    • 0026343441 scopus 로고
    • Suppression of the abnormal phenotype of Salmonella typhimurium rfaH mutants by mutations in the gene for transcription termination factor Rho
    • Farewell, A., Brazas, R., Davie, E., Mason, J. Rothfield, L.I. (1991) Suppression of the abnormal phenotype of Salmonella typhimurium rfaH mutants by mutations in the gene for transcription termination factor Rho. J Bacteriol 173 : 5188 5193.
    • (1991) J Bacteriol , vol.173 , pp. 5188-5193
    • Farewell, A.1    Brazas, R.2    Davie, E.3    Mason, J.4    Rothfield, L.I.5
  • 15
    • 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. 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
  • 16
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • DOI 10.1016/j.molcel.2004.11.040, PII S1097276504007300
    • Kettenberger, H., Armache, K.J. Cramer, P. (2004) Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol Cell 16 : 955 965. (Pubitemid 40018405)
    • (2004) Molecular Cell , vol.16 , Issue.6 , pp. 955-965
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 17
    • 0023914286 scopus 로고
    • Expression of the E. coli hemolysin secretion gene hlyB involves transcript anti-termination within the hly operon
    • Koronakis, V., Cross, M. Hughes, C. (1988) Expression of the E. coli hemolysin secretion gene hlyB involves transcript anti-termination within the hly operon. Nucleic Acids Res 16 : 4789 4800.
    • (1988) Nucleic Acids Res , vol.16 , pp. 4789-4800
    • Koronakis, V.1    Cross, M.2    Hughes, C.3
  • 19
    • 0029935766 scopus 로고    scopus 로고
    • RfaH enhances elongation of Escherichia coli hlyCABD mRNA
    • Leeds, J.A. Welch, R.A. (1996) RfaH enhances elongation of Escherichia coli hlyCABD mRNA. J Bacteriol 178 : 1850 1857.
    • (1996) J Bacteriol , vol.178 , pp. 1850-1857
    • Leeds, J.A.1    Welch, R.A.2
  • 21
    • 67650676737 scopus 로고    scopus 로고
    • Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators
    • Mooney, R.A., Schweimer, K., Rosch, P., Gottesman, M. Landick, R. (2009b) Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J Mol Biol 391 : 341 358.
    • (2009) J Mol Biol , vol.391 , pp. 341-358
    • Mooney, R.A.1    Schweimer, K.2    Rosch, P.3    Gottesman, M.4    Landick, R.5
  • 23
    • 0036076368 scopus 로고    scopus 로고
    • Loss of regulatory protein RfaH attenuates virulence of uropathogenic Escherichia coli
    • DOI 10.1128/IAI.70.8.4406-4413.2002
    • Nagy, G., Dobrindt, U., Schneider, G., Khan, A.S., Hacker, J. Emody, L. (2002) Loss of regulatory protein RfaH attenuates virulence of uropathogenic Escherichia coli. Infect Immun 70 : 4406 4413. (Pubitemid 34790951)
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4406-4413
    • Nagy, G.1    Dobrindt, U.2    Schneider, G.3    Khan, A.S.4    Hacker, J.5    Emody, L.6
  • 24
    • 33749258050 scopus 로고    scopus 로고
    • Down-regulation of key virulence factors makes the Salmonella enterica serovar typhimurium rfaH mutant a promising live-attenuated vaccine candidate
    • DOI 10.1128/IAI.00619-06
    • Nagy, G., Danino, V., Dobrindt, U., Pallen, M., Chaudhuri, R., Emody, L., et al. (2006) Down-regulation of key virulence factors makes the Salmonella enterica serovar Typhimurium rfaH mutant a promising live-attenuated vaccine candidate. Infect Immun 74 : 5914 5925. (Pubitemid 44484579)
    • (2006) Infection and Immunity , vol.74 , Issue.10 , pp. 5914-5925
    • Nagy, G.1    Danino, V.2    Dobrindt, U.3    Pallen, M.4    Chaudhuri, R.5    Emody, L.6    Hinton, J.C.7    Hacker, J.8
  • 25
    • 57349097787 scopus 로고    scopus 로고
    • Genetic assays to define and characterize protein-protein interactions involved in gene regulation
    • Nickels, B.E. (2009) Genetic assays to define and characterize protein-protein interactions involved in gene regulation. Methods 47 : 53 62.
    • (2009) Methods , vol.47 , pp. 53-62
    • Nickels, B.E.1
  • 26
    • 0037326242 scopus 로고    scopus 로고
    • Transcriptional organization and regulation of the Escherichia coli K30 group 1 capsule biosynthesis (cps) gene cluster
    • DOI 10.1046/j.1365-2958.2003.03354.x
    • Rahn, A. Whitfield, C. (2003) Transcriptional organization and regulation of the Escherichia coli K30 group 1 capsule biosynthesis (cps) gene cluster. Mol Microbiol 47 : 1045 1060. (Pubitemid 36232800)
    • (2003) Molecular Microbiology , vol.47 , Issue.4 , pp. 1045-1060
    • Rahn, A.1    Whitfield, C.2
  • 27
    • 20444410362 scopus 로고    scopus 로고
    • Identification of a structural element that is essential for two functions of transcription factor NusG
    • Richardson, L.V. Richardson, J.P. (2005) Identification of a structural element that is essential for two functions of transcription factor NusG. Biochim Biophys Acta 1729 : 135 140.
    • (2005) Biochim Biophys Acta , vol.1729 , pp. 135-140
    • Richardson, L.V.1    Richardson, J.P.2
  • 29
    • 0037009445 scopus 로고    scopus 로고
    • Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities
    • DOI 10.1093/emboj/cdf455
    • Steiner, T., Kaiser, J.T., Marinkovic, S., Huber, R. Wahl, M.C. (2002) Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities. EMBO J 21 : 4641 4653. (Pubitemid 34984351)
    • (2002) EMBO Journal , vol.21 , Issue.17 , pp. 4641-4653
    • Steiner, T.1    Kaiser, J.T.2    Marinkovic, S.3    Huber, R.4    Wahl, M.C.5
  • 30
    • 0028171277 scopus 로고
    • Regulation of Escherichia coli K5 capsular polysaccharide expression: Evidence for involvement of RfaH in the expression of group II capsules
    • DOI 10.1016/0378-1097(94)90338-7
    • Stevens, M.P., Hanfling, P., Jann, B., Jann, K. Roberts, I.S. (1994) Regulation of Escherichia coli K5 capsular polysaccharide expression: evidence for involvement of RfaH in the expression of group II capsules. FEMS Microbiol Lett 124 : 93 98. (Pubitemid 2164237)
    • (1994) FEMS Microbiology Letters , vol.124 , Issue.1 , pp. 93-98
    • Stevens, M.P.1    Hanfling, P.2    Jann, B.3    Jann, K.4    Roberts, I.S.5
  • 31
    • 0026527997 scopus 로고
    • Requirement for E. coli NusG protein in factor-dependent transcription termination
    • Sullivan, S.L. Gottesman, M.E. (1992) Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell 68 : 989 994.
    • (1992) Cell , vol.68 , pp. 989-994
    • Sullivan, S.L.1    Gottesman, M.E.2
  • 32
  • 33
    • 67449116330 scopus 로고    scopus 로고
    • Structural basis of transcription: Mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA
    • Sydow, J.F., Brueckner, F., Cheung, A.C., Damsma, G.E., Dengl, S., Lehmann, E., et al. (2009) Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Mol Cell 34 : 710 721.
    • (2009) Mol Cell , vol.34 , pp. 710-721
    • Sydow, J.F.1    Brueckner, F.2    Cheung, A.C.3    Damsma, G.E.4    Dengl, S.5    Lehmann, E.6
  • 34
    • 1342325469 scopus 로고    scopus 로고
    • In Vivo Effect of NusB and NusG on rRNA Transcription Antitermination
    • DOI 10.1128/JB.186.5.1304-1310.2004
    • Torres, M., Balada, J.M., Zellars, M., Squires, C. Squires, C.L. (2004) In vivo effect of NusB and NusG on rRNA transcription antitermination. J Bacteriol 186 : 1304 1310. (Pubitemid 38248719)
    • (2004) Journal of Bacteriology , vol.186 , Issue.5 , pp. 1304-1310
    • Torres, M.1    Balada, J.-M.2    Zellars, M.3    Squires, C.4    Squires, C.L.5
  • 35
    • 34547204502 scopus 로고    scopus 로고
    • A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing
    • DOI 10.1016/j.molcel.2007.06.008, PII S1097276507003747
    • Toulokhonov, I., Zhang, J., Palangat, M. Landick, R. (2007) A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol Cell 27 : 406 419. (Pubitemid 47126936)
    • (2007) Molecular Cell , vol.27 , Issue.3 , pp. 406-419
    • Toulokhonov, I.1    Zhang, J.2    Palangat, M.3    Landick, R.4
  • 36
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6. a resolution
    • DOI 10.1038/nature752
    • Vassylyev, D.G., Sekine, S., Laptenko, O., Lee, J., Vassylyeva, M.N., Borukhov, S. Yokoyama, S. (2002) Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 a resolution. Nature 417 : 712 719. (Pubitemid 34640620)
    • (2002) Nature , vol.417 , Issue.6890 , pp. 712-719
    • Vassylyev, D.G.1    Sekine, S.-I.2    Laptenko, O.3    Lee, J.4    Vassylyeva, M.N.5    Borukhov, S.6    Yokoyama, S.7
  • 37
    • 34447499995 scopus 로고    scopus 로고
    • Structural basis for transcription elongation by bacterial RNA polymerase
    • DOI 10.1038/nature05932, PII NATURE05932
    • Vassylyev, D.G., Vassylyeva, M.N., Perederina, A., Tahirov, T.H. Artsimovitch, I. (2007) Structural basis for transcription elongation by bacterial RNA polymerase. Nature 448 : 157 162. (Pubitemid 47067370)
    • (2007) Nature , vol.448 , Issue.7150 , pp. 157-162
    • Vassylyev, D.G.1    Vassylyeva, M.N.2    Perederina, A.3    Tahirov, T.H.4    Artsimovitch, I.5
  • 39
    • 0027404233 scopus 로고
    • Involvement of lipopolysaccharide in the secretion of Escherichia coli α-haemolysin and Erwinia chrysanthemi proteases
    • DOI 10.1111/j.1365-2958.1993.tb01105.x
    • Wandersman, C. Letoffe, S. (1993) Involvement of lipopolysaccharide in the secretion of Escherichia coli alpha-haemolysin and Erwinia chrysanthemi proteases. Mol Microbiol 7 : 141 150. (Pubitemid 23011104)
    • (1993) Molecular Microbiology , vol.7 , Issue.1 , pp. 141-150
    • Wandersman, C.1    Letoffe, S.2
  • 40
    • 0031058485 scopus 로고    scopus 로고
    • Nuclease cleavage of the upstream half of the nontemplate strand DNA in an Escherichia coli transcription elongation complex causes upstream translocation and transcriptional arrest
    • DOI 10.1074/jbc.272.9.5989
    • Wang, D. Landick, R. (1997) Nuclease cleavage of the upstream half of the nontemplate strand DNA in an Escherichia coli transcription elongation complex causes upstream translocation and transcriptional arrest. J Biol Chem 272 : 5989 5994. (Pubitemid 27102437)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5989-5994
    • Wang, D.1    Landick, R.2
  • 41
    • 0032526404 scopus 로고    scopus 로고
    • Engineering the luxCDABE genes from Photorhabdus luminescens to provide a bioluminescent reporter for constitutive and promoter probe plasmids and mini-Tn5 constructs
    • DOI 10.1016/S0378-1097(98)00173-6, PII S0378109798001736
    • Winson, M.K., Swift, S., Hill, P.J., Sims, C.M., Griesmayr, G., Bycroft, B.W., et al. (1998) Engineering the luxCDABE genes from Photorhabdus luminescens to provide a bioluminescent reporter for constitutive and promoter probe plasmids and mini-Tn5 constructs. FEMS Microbiol Lett 163 : 193 202. (Pubitemid 28289358)
    • (1998) FEMS Microbiology Letters , vol.163 , Issue.2 , pp. 193-202
    • Winson, M.K.1    Swift, S.2    Hill, P.J.3    Sims, C.M.4    Griesmayr, G.5    Bycroft, B.W.6    Williams, P.7    Stewart, G.S.A.B.8
  • 42
    • 0036275511 scopus 로고    scopus 로고
    • Requirement for NusG for transcription antitermination in vivo by the lambda N protein
    • Zhou, Y., Filter, J.J., Court, D.L., Gottesman, M.E. Friedman, D.I. (2002) Requirement for NusG for transcription antitermination in vivo by the lambda N protein. J Bacteriol 184 : 3416 3418.
    • (2002) J Bacteriol , vol.184 , pp. 3416-3418
    • Zhou, Y.1    Filter, J.J.2    Court, D.L.3    Gottesman, M.E.4    Friedman, D.I.5


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