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Volumn 41, Issue 22, 2013, Pages 10077-10085

Interdomain contacts control folding of transcription factor RfaH

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RFAH; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84890367793     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt779     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 84857625656 scopus 로고    scopus 로고
    • A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life
    • Werner, F. (2012) A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life. J. Mol. Biol., 417, 13-27.
    • (2012) J. Mol. Biol. , vol.417 , pp. 13-27
    • Werner, F.1
  • 2
    • 0030718529 scopus 로고    scopus 로고
    • RfaH and the ops element components of a novel system controlling bacterial transcription elongation
    • Bailey, M.J., Hughes, C. and Koronakis, V. (1997) RfaH and the ops element, components of a novel system controlling bacterial transcription elongation. Mol. Microbiol., 26, 845-851.
    • (1997) Mol. Microbiol , vol.26 , pp. 845-851
    • Bailey, M.J.1    Hughes, C.2    Koronakis, V.3
  • 3
    • 0036076368 scopus 로고    scopus 로고
    • Loss of regulatory protein RfaH attenuates virulence of uropathogenic Escherichia coli
    • Nagy, G., Dobrindt, U., Schneider, G., Khan, A.S., Hacker, J. and Emody, L. (2002) Loss of regulatory protein RfaH attenuates virulence of uropathogenic Escherichia coli. Infect. Immun., 70, 4406-4413.
    • (2002) Infect. Immun , vol.70 , pp. 4406-4413
    • Nagy, G.1    Dobrindt, U.2    Schneider, G.3    Khan, A.S.4    Hacker, J.5    Emody, L.6
  • 4
    • 0037133970 scopus 로고    scopus 로고
    • The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand
    • Artsimovitch, I. and Landick, R. (2002) The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell, 109, 193-203.
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 5
  • 7
    • 79960449643 scopus 로고    scopus 로고
    • The beta subunit gate loop is required for RNA polymerase modification by RfaH and NusG
    • Sevostyanova, A., Belogurov, G.A., Mooney, R.A., Landick, R. and Artsimovitch, I. (2011) The beta subunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol. Cell, 43, 253-262.
    • (2011) Mol. Cell , vol.43 , pp. 253-262
    • Sevostyanova, A.1    Belogurov, G.A.2    Mooney, R.A.3    Landick, R.4    Artsimovitch, I.5
  • 8
    • 0029935766 scopus 로고    scopus 로고
    • RfaH enhances elongation of Escherichia coli hlyCABD mRNA
    • Leeds, J.A. and 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
  • 10
    • 79954470299 scopus 로고    scopus 로고
    • Domain interactions of the transcription-translation coupling factor Escherichia coli NusG are intermolecular and transient
    • Burmann, B.M., Scheckenhofer, U., Schweimer, K. and Rosch, P. (2011) Domain interactions of the transcription-translation coupling factor Escherichia coli NusG are intermolecular and transient. Biochem. J., 435, 783-789.
    • (2011) Biochem. J. , vol.435 , pp. 783-789
    • Burmann, B.M.1    Scheckenhofer, U.2    Schweimer, K.3    Rosch, P.4
  • 15
    • 79551690253 scopus 로고    scopus 로고
    • Folding at the birth of the nascent chain: Coordinating translation with co-translational folding
    • Zhang, G. and Ignatova, Z. (2011) Folding at the birth of the nascent chain: coordinating translation with co-translational folding. Curr. Opin. Struct. Biol., 21, 25-31.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 25-31
    • Zhang, G.1    Ignatova, Z.2
  • 17
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B.A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol., 278, 313-352.
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 18
  • 21
    • 38949110771 scopus 로고    scopus 로고
    • The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex
    • Sevostyanova, A., Svetlov, V., Vassylyev, D.G. and Artsimovitch, I. (2008) The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex. Proc. Natl Acad. Sci. USA, 105, 865-870.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 865-870
    • Sevostyanova, A.1    Svetlov, V.2    Vassylyev, D.G.3    Artsimovitch, I.4
  • 22
    • 84869761071 scopus 로고    scopus 로고
    • The protein-folding problem, 50 years on
    • Dill, K.A. and MacCallum, J.L. (2012) The protein-folding problem, 50 years on. Science, 338, 1042-1046.
    • (2012) Science , vol.338 , pp. 1042-1046
    • Dill, K.A.1    MacCallum, J.L.2
  • 23
    • 29444445833 scopus 로고    scopus 로고
    • Sequence determinants of a conformational switch in a protein structure
    • Anderson, T.A., Cordes, M.H. and Sauer, R.T. (2005) Sequence determinants of a conformational switch in a protein structure. Proc. Natl Acad. Sci. USA, 102, 18344-18349.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18344-18349
    • Anderson, T.A.1    Cordes, M.H.2    Sauer, R.T.3
  • 24
    • 75849116590 scopus 로고    scopus 로고
    • A minimal sequence code for switching protein structure and function
    • Alexander, P.A., He, Y., Chen, Y., Orban, J. and Bryan, P.N. (2009) A minimal sequence code for switching protein structure and function. Proc. Natl Acad. Sci. USA, 106, 21149-21154.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21149-21154
    • Alexander, P.A.1    He, Y.2    Chen, Y.3    Orban, J.4    Bryan, P.N.5
  • 27
    • 84861315209 scopus 로고    scopus 로고
    • High-resolution structure of infectious prion protein: The final frontier
    • Diaz-Espinoza, R. and Soto, C. (2012) High-resolution structure of infectious prion protein: the final frontier. Nat. Struct. Mol. Biol., 19, 370-377.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 370-377
    • Diaz-Espinoza, R.1    Soto, C.2
  • 28
    • 84862848780 scopus 로고    scopus 로고
    • Ribosome-associated chaperones as key players in proteostasis
    • Preissler, S. and Deuerling, E. (2012) Ribosome-associated chaperones as key players in proteostasis. Trends Biochem. Sci., 37, 274-283.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 274-283
    • Preissler, S.1    Deuerling, E.2
  • 30
    • 34447095724 scopus 로고    scopus 로고
    • Molecular gymnastics: Serpin structure folding and misfolding
    • Whisstock, J.C. and Bottomley, S.P. (2006) Molecular gymnastics: serpin structure, folding and misfolding. Curr. Opin. Struct. Biol., 16, 761-768.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 761-768
    • Whisstock, J.C.1    Bottomley, S.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.