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Volumn 43, Issue 2, 2011, Pages 253-262

The β Subunit Gate Loop Is Required for RNA Polymerase Modification by RfaH and NusG

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; RFAH PROTEIN; RNA POLYMERASE BETA SUBUNIT; UNCLASSIFIED DRUG;

EID: 79960449643     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2011.05.026     Document Type: Article
Times cited : (88)

References (49)
  • 1
    • 0034691146 scopus 로고    scopus 로고
    • Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
    • Artsimovitch I., Landick R. Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc. Natl. Acad. Sci. USA 2000, 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
    • The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand
    • Artsimovitch I., Landick R. The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell 2002, 109:193-203.
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 3
    • 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. In vitro recruitment of the RfaH regulatory protein into a specialised transcription complex, directed by the nucleic acid ops element. Mol. Gen. Genet. 2000, 262:1052-1059.
    • (2000) Mol. Gen. Genet. , vol.262 , pp. 1052-1059
    • Bailey, M.J.1    Hughes, C.2    Koronakis, V.3
  • 7
    • 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. RNA-directed DNA methylation requires an AGO4-interacting member of the SPT5 elongation factor family. EMBO Rep. 2009, 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
    • 1942539312 scopus 로고    scopus 로고
    • Highly divergent RfaH orthologs from pathogenic proteobacteria can substitute for Escherichia coli RfaH both in vivo and in vitro
    • Carter H.D., Svetlov V., Artsimovitch I. Highly divergent RfaH orthologs from pathogenic proteobacteria can substitute for Escherichia coli RfaH both in vivo and in vitro. J. Bacteriol. 2004, 186:2829-2840.
    • (2004) J. Bacteriol. , vol.186 , pp. 2829-2840
    • Carter, H.D.1    Svetlov, V.2    Artsimovitch, I.3
  • 11
    • 34249941797 scopus 로고    scopus 로고
    • Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymerase
    • Davis C.A., Bingman C.A., Landick R., Record M.T., Saecker R.M. Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymerase. Proc. Natl. Acad. Sci. USA 2007, 104:7833-7838.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7833-7838
    • Davis, C.A.1    Bingman, C.A.2    Landick, R.3    Record, M.T.4    Saecker, R.M.5
  • 12
    • 32044451311 scopus 로고    scopus 로고
    • Functional interplay between the jaw domain of bacterial RNA polymerase and allele-specific residues in the product RNA-binding pocket
    • Ederth J., Mooney R.A., Isaksson L.A., Landick R. Functional interplay between the jaw domain of bacterial RNA polymerase and allele-specific residues in the product RNA-binding pocket. J. Mol. Biol. 2006, 356:1163-1179.
    • (2006) J. Mol. Biol. , vol.356 , pp. 1163-1179
    • Ederth, J.1    Mooney, R.A.2    Isaksson, L.A.3    Landick, R.4
  • 13
    • 74549191169 scopus 로고    scopus 로고
    • An allosteric mechanism of Rho-dependent transcription termination
    • Epshtein V., Dutta D., Wade J., Nudler E. An allosteric mechanism of Rho-dependent transcription termination. Nature 2010, 463:245-249.
    • (2010) Nature , vol.463 , pp. 245-249
    • Epshtein, V.1    Dutta, D.2    Wade, J.3    Nudler, E.4
  • 14
    • 78649527702 scopus 로고    scopus 로고
    • The bridge helix coordinates movements of modules in RNA polymerase
    • Hein P.P., Landick R. The bridge helix coordinates movements of modules in RNA polymerase. BMC Biol. 2010, 8:144.
    • (2010) BMC Biol. , vol.8 , pp. 144
    • Hein, P.P.1    Landick, R.2
  • 17
    • 0035368724 scopus 로고    scopus 로고
    • RNA polymerase clamps down
    • Landick R. RNA polymerase clamps down. Cell 2001, 105:567-570.
    • (2001) Cell , vol.105 , pp. 567-570
    • Landick, R.1
  • 18
    • 0029834733 scopus 로고    scopus 로고
    • Quantitative analysis of transcriptional pausing by Escherichia coli RNA polymerase: his leader pause site as paradigm
    • Landick R., Wang D., Chan C.L. Quantitative analysis of transcriptional pausing by Escherichia coli RNA polymerase: his leader pause site as paradigm. Methods Enzymol. 1996, 274:334-353.
    • (1996) Methods Enzymol. , vol.274 , pp. 334-353
    • Landick, R.1    Wang, D.2    Chan, C.L.3
  • 19
    • 79953779997 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity
    • Martinez-Rucobo F.W., Sainsbury S., Cheung A.C., Cramer P. Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity. EMBO J. 2011, 30:1302-1310.
    • (2011) EMBO J. , vol.30 , pp. 1302-1310
    • Martinez-Rucobo, F.W.1    Sainsbury, S.2    Cheung, A.C.3    Cramer, P.4
  • 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., Rösch P., Gottesman M., Landick R. Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J. Mol. Biol. 2009, 391:341-358.
    • (2009) J. Mol. Biol. , vol.391 , pp. 341-358
    • Mooney, R.A.1    Schweimer, K.2    Rösch, P.3    Gottesman, M.4    Landick, R.5
  • 22
    • 0021262602 scopus 로고
    • Specificity of release by Escherichia coli transcription termination factor rho of nascent mRNA transcripts initiated at the lambda PR
    • Morgan W.D., Bear D.G., von Hippel P.H. Specificity of release by Escherichia coli transcription termination factor rho of nascent mRNA transcripts initiated at the lambda PR. J. Biol. Chem. 1984, 259:8664-8671.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8664-8671
    • Morgan, W.D.1    Bear, D.G.2    von Hippel, P.H.3
  • 24
    • 0345047725 scopus 로고    scopus 로고
    • Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking
    • Neuman K.C., Abbondanzieri E.A., Landick R., Gelles J., Block S.M. Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking. Cell 2003, 115:437-447.
    • (2003) Cell , vol.115 , pp. 437-447
    • Neuman, K.C.1    Abbondanzieri, E.A.2    Landick, R.3    Gelles, J.4    Block, S.M.5
  • 25
    • 57349097787 scopus 로고    scopus 로고
    • Genetic assays to define and characterize protein-protein interactions involved in gene regulation
    • Nickels B.E. Genetic assays to define and characterize protein-protein interactions involved in gene regulation. Methods 2009, 47:53-62.
    • (2009) Methods , vol.47 , pp. 53-62
    • Nickels, B.E.1
  • 26
    • 33746403681 scopus 로고    scopus 로고
    • Controlling the elongation phase of transcription with P-TEFb
    • Peterlin B.M., Price D.H. Controlling the elongation phase of transcription with P-TEFb. Mol. Cell 2006, 23:297-305.
    • (2006) Mol. Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 28
    • 77951589688 scopus 로고    scopus 로고
    • Cooperation between translating ribosomes and RNA polymerase in transcription elongation
    • Proshkin S., Rahmouni A.R., Mironov A., Nudler E. Cooperation between translating ribosomes and RNA polymerase in transcription elongation. Science 2010, 328:504-508.
    • (2010) Science , vol.328 , pp. 504-508
    • Proshkin, S.1    Rahmouni, A.R.2    Mironov, A.3    Nudler, E.4
  • 29
    • 0031558773 scopus 로고    scopus 로고
    • Regulation of the elongation-termination decision at intrinsic terminators by antitermination protein N of phage lambda
    • Rees W.A., Weitzel S.E., Das A., von Hippel P.H. Regulation of the elongation-termination decision at intrinsic terminators by antitermination protein N of phage lambda. J. Mol. Biol. 1997, 273:797-813.
    • (1997) J. Mol. Biol. , vol.273 , pp. 797-813
    • Rees, W.A.1    Weitzel, S.E.2    Das, A.3    von Hippel, P.H.4
  • 30
    • 0016795582 scopus 로고
    • Transcription termination factor Rho activity is altered in Escherichia coli with SuA gene mutations
    • Richardson J.P., Grimley C., Lowery C. Transcription termination factor Rho activity is altered in Escherichia coli with SuA gene mutations. Proc. Natl. Acad. Sci. USA 1975, 72:1725-1728.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1725-1728
    • Richardson, J.P.1    Grimley, C.2    Lowery, C.3
  • 34
    • 78649866419 scopus 로고    scopus 로고
    • Functional analysis of Thermus thermophilus transcription factor NusG
    • Sevostyanova A., Artsimovitch I. Functional analysis of Thermus thermophilus transcription factor NusG. Nucleic Acids Res. 2010, 38:7432-7445.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7432-7445
    • Sevostyanova, A.1    Artsimovitch, I.2
  • 35
    • 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., Artsimovitch I. The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex. Proc. Natl. Acad. Sci. USA 2008, 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
  • 36
    • 0027463435 scopus 로고
    • Ribosomal RNA antitermination in vitro: requirement for Nus factors and one or more unidentified cellular components
    • Squires C.L., Greenblatt J., Li J., Condon C., Squires C.L. Ribosomal RNA antitermination in vitro: requirement for Nus factors and one or more unidentified cellular components. Proc. Natl. Acad. Sci. USA 1993, 90:970-974.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 970-974
    • Squires, C.L.1    Greenblatt, J.2    Li, J.3    Condon, C.4    Squires, C.L.5
  • 37
    • 0030852077 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli K5 capsule gene cluster by transcription antitermination
    • Stevens M.P., Clarke B.R., Roberts I.S. Regulation of the Escherichia coli K5 capsule gene cluster by transcription antitermination. Mol. Microbiol. 1997, 24:1001-1012.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1001-1012
    • Stevens, M.P.1    Clarke, B.R.2    Roberts, I.S.3
  • 38
    • 79953792360 scopus 로고    scopus 로고
    • Clamping the clamp of RNA polymerase
    • Svetlov V., Nudler E. Clamping the clamp of RNA polymerase. EMBO J. 2011, 30:1190-1191.
    • (2011) EMBO J. , vol.30 , pp. 1190-1191
    • Svetlov, V.1    Nudler, E.2
  • 40
    • 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., Vassylyev D., Cramer P. Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Mol. Cell 2009, 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    Vassylyev, D.7    Cramer, P.8
  • 42
    • 34547204502 scopus 로고    scopus 로고
    • A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing
    • Toulokhonov I., Zhang J., Palangat M., Landick R. A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol. Cell 2007, 27:406-419.
    • (2007) Mol. Cell , vol.27 , pp. 406-419
    • Toulokhonov, I.1    Zhang, J.2    Palangat, M.3    Landick, R.4
  • 45
    • 67349151383 scopus 로고    scopus 로고
    • SPT5-like, a new component in plant RdDM
    • Wang M.B., Dennis E.S. SPT5-like, a new component in plant RdDM. EMBO Rep. 2009, 10:573-575.
    • (2009) EMBO Rep. , vol.10 , pp. 573-575
    • Wang, M.B.1    Dennis, E.S.2
  • 46
    • 77958579653 scopus 로고    scopus 로고
    • The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
    • Weinzierl R.O. The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain. BMC Biol. 2010, 8:134.
    • (2010) BMC Biol. , vol.8 , pp. 134
    • Weinzierl, R.O.1
  • 47
    • 0033597435 scopus 로고    scopus 로고
    • Mechanism of intrinsic transcription termination and antitermination
    • Yarnell W.S., Roberts J.W. Mechanism of intrinsic transcription termination and antitermination. Science 1999, 284:611-615.
    • (1999) Science , vol.284 , pp. 611-615
    • Yarnell, W.S.1    Roberts, J.W.2
  • 48
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 1999, 98:811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 49
    • 77449093660 scopus 로고    scopus 로고
    • Role of the RNA polymerase trigger loop in catalysis and pausing
    • Zhang J., Palangat M., Landick R. Role of the RNA polymerase trigger loop in catalysis and pausing. Nat. Struct. Mol. Biol. 2010, 17:99-104.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 99-104
    • Zhang, J.1    Palangat, M.2    Landick, R.3


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