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Volumn 30, Issue 7, 2011, Pages 1302-1310

Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity

Author keywords

gene regulation; gene transcription; multiprotein complex structure; RNA polymerase elongation; transcription elongation factor

Indexed keywords

PROTEIN SPT4; PROTEIN SPT5; REPRESSOR PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 79953779997     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.64     Document Type: Article
Times cited : (195)

References (62)
  • 5
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond CS, Schuttelkopf AW (2009) ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr D Biol Crystallogr 65: 510-512
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 510-512
    • Bond, C.S.1    Schuttelkopf, A.W.2
  • 7
    • 0028905513 scopus 로고
    • Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro
    • Burova E, Hung SC, Sagitov V, Stitt BL, Gottesman ME (1995) Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro. J Bacteriol 177: 1388-1392
    • (1995) J Bacteriol , vol.177 , pp. 1388-1392
    • Burova, E.1    Hung, S.C.2    Sagitov, V.3    Stitt, B.L.4    Gottesman, M.E.5
  • 8
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms
    • DOI 10.1126/science.1090838
    • Bushnell DA, Westover KD, Davis RE, Kornberg RD (2004) Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms. Science 303: 983-988 (Pubitemid 38209696)
    • (2004) Science , vol.303 , Issue.5660 , pp. 983-988
    • Bushnell, D.A.1    Westover, K.D.2    Davis, R.E.3    Kornberg, R.D.4
  • 9
    • 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 CJ, Washburn RS, Tadigotla VR, Brown LM, Gottesman ME, 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
  • 10
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4
    • CCP4 (1994) The CCP4 Suite: programs for protein crystallography. Acta Cryst D50: 760-763
    • (1994) Acta Cryst D , vol.50 , pp. 760-763
  • 11
    • 70349149449 scopus 로고    scopus 로고
    • Repression of RNA polymerase II elongation in vivo is critically dependent on the C-terminus of Spt5
    • Chen H, Contreras X, Yamaguchi Y, Handa H, Peterlin BM, Guo S (2009) Repression of RNA polymerase II elongation in vivo is critically dependent on the C-terminus of Spt5. PLoS One 4: e6918
    • (2009) PLoS One , vol.4
    • Chen, H.1    Contreras, X.2    Yamaguchi, Y.3    Handa, H.4    Peterlin, B.M.5    Guo, S.6
  • 12
    • 34547683177 scopus 로고    scopus 로고
    • The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex
    • DOI 10.1038/nsmb1272, PII NSMB1272
    • Chen H-T, Warfield L, Hahn S (2007) The positions of TFIIF and TFIIE in the RNA polymerase II transcription initiation complex. Nat Struct Mol Biol 8: 696-703 (Pubitemid 47220058)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.8 , pp. 696-703
    • Chen, H.-T.1    Warfield, L.2    Hahn, S.3
  • 14
    • 56649106687 scopus 로고    scopus 로고
    • Analysis of factor interactions with RNA polymerase II elongation complexes using a new electrophoretic mobility shift assay
    • Cheng B, Price DH (2008) Analysis of factor interactions with RNA polymerase II elongation complexes using a new electrophoretic mobility shift assay. Nucleic Acids Res 36: e135
    • (2008) Nucleic Acids Res , vol.36
    • Cheng, B.1    Price, D.H.2
  • 15
    • 25144510935 scopus 로고    scopus 로고
    • Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase β′ subunit
    • DOI 10.1016/j.jmb.2005.07.073, PII S0022283605008995
    • Chlenov M, Masuda S, Murakami KS, Nikiforov V, Darst SA, Mustaev A (2005) Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase beta' sub-unit. J Mol Biol 353: 138-154 (Pubitemid 41338846)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.1 , pp. 138-154
    • Chlenov, M.1    Masuda, S.2    Murakami, K.S.3    Nikiforov, V.4    Darst, S.A.5    Mustaev, A.6
  • 18
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • DOI 10.1126/science.1059493
    • Cramer P, Bushnell DA, Kornberg RD (2001) Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292: 1863-1876 (Pubitemid 32538356)
    • (2001) Science , vol.292 , Issue.5523 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 20
    • 78651481313 scopus 로고    scopus 로고
    • Cycling through transcription with the RNA polymerase F/E (RPB4/7) complex: Structure, function and evolution of archaeal RNA polymerase
    • Grohmann D, Werner F (2011) Cycling through transcription with the RNA polymerase F/E (RPB4/7) complex: structure, function and evolution of archaeal RNA polymerase. Res Microbiol 162: 10-18
    • (2011) Res Microbiol , vol.162 , pp. 10-18
    • Grohmann, D.1    Werner, F.2
  • 21
    • 55249117324 scopus 로고    scopus 로고
    • Core structure of the yeast spt4-spt5 complex: A conserved module for regulation of transcription elongation
    • Guo M, Xu F, Yamada J, Egelhofer T, Gao Y, Hartzog GA, Teng M, Niu L (2008) Core structure of the yeast spt4-spt5 complex: a conserved module for regulation of transcription elongation. Structure 16: 1649-1658
    • (2008) Structure , vol.16 , pp. 1649-1658
    • Guo, M.1    Xu, F.2    Yamada, J.3    Egelhofer, T.4    Gao, Y.5    Hartzog, G.A.6    Teng, M.7    Niu, L.8
  • 23
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog GA, Wada T, Handa H, Winston F (1998) Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev 12: 357-369 (Pubitemid 28084264)
    • (1998) Genes and Development , vol.12 , Issue.3 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 24
    • 39149142997 scopus 로고    scopus 로고
    • The X-ray crystal structure of RNA polymerase from Archaea
    • DOI 10.1038/nature06530, PII NATURE06530
    • Hirata A, Klein BJ, Murakami KS (2008) The X-ray crystal structure of RNA polymerase from Archaea. Nature 451: 851-854 (Pubitemid 351253162)
    • (2008) Nature , vol.451 , Issue.7180 , pp. 851-854
    • Hirata, A.1    Klein, B.J.2    Murakami, K.S.3
  • 28
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • DOI 10.1016/S0092-8674(03)00598-1
    • Kettenberger H, Armache K-J, Cramer P (2003) Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114: 347-357 (Pubitemid 36962933)
    • (2003) Cell , vol.114 , Issue.3 , pp. 347-357
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 29
    • 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
  • 31
    • 0242515770 scopus 로고    scopus 로고
    • A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants
    • DOI 10.1021/bi0272508
    • Knowlton JR, Bubunenko M, Andrykovitch M, Guo W Routzahn KM, Waugh DS, Court DL, Ji X (2003) A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallo-graphy and supported by site-directed mutants. Biochemistry 42: 2275-2281 (Pubitemid 36255201)
    • (2003) Biochemistry , vol.42 , Issue.8 , pp. 2275-2281
    • Knowlton, J.R.1    Bubunenko, M.2    Andrykovitch, M.3    Guo, W.4    Routzahn, K.M.5    Waugh, D.S.6    Court, D.L.7    Ji, X.8
  • 35
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG (2006) The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 62: 48-57
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 36
    • 74249102477 scopus 로고    scopus 로고
    • Structure of an RNA polymerase II-TFIIB complex and the trans-cription initiation mechanism
    • Liu X, Bushnell DA, Wang D, Calero G, Kornberg RD (2010) Structure of an RNA polymerase II-TFIIB complex and the trans-cription initiation mechanism. Science 327: 206-209
    • (2010) Science , vol.327 , pp. 206-209
    • Liu, X.1    Bushnell, D.A.2    Wang, D.3    Calero, G.4    Kornberg, R.D.5
  • 37
    • 68849086180 scopus 로고    scopus 로고
    • Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruit-ment of the PAF complex
    • Liu Y, Warfield L, Zhang C, Luo J, Allen J, Lang WH, Ranish J, Shokat KM, Hahn S (2009) Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruit-ment of the PAF complex. Mol Cell Biol 29: 4852-4863
    • (2009) Mol Cell Biol , vol.29 , pp. 4852-4863
    • Liu, Y.1    Warfield, L.2    Zhang, C.3    Luo, J.4    Allen, J.5    Lang, W.H.6    Ranish, J.7    Shokat, K.M.8    Hahn, S.9
  • 40
    • 77954889072 scopus 로고    scopus 로고
    • Interactions between DSIF (DRB sensitivity inducing factor), NELF (negative elongation factor), and the Drosophila RNA polymerase II transcription elongation complex
    • Missra A, Gilmour DS (2010) Interactions between DSIF (DRB sensitivity inducing factor), NELF (negative elongation factor), and the Drosophila RNA polymerase II transcription elongation complex. Proc Natl Acad Sci USA 107: 11301-11306
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11301-11306
    • Missra, A.1    Gilmour, D.S.2
  • 41
    • 67650676737 scopus 로고    scopus 로고
    • Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymer-ase and regulators
    • Mooney RA, Schweimer K, Rosch P, Gottesman M, Landick R (2009) Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymer-ase 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
  • 42
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • DOI 10.1126/science.1069595
    • Murakami KS, Masuda S, Campbell EA, Muzzin O, Darst SA (2002a) Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 296: 1285-1290 (Pubitemid 34522778)
    • (2002) Science , vol.296 , Issue.5571 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 43
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • DOI 10.1126/science.1069594
    • Murakami KS, Masuda S, Darst SA (2002b) Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution. Science 296: 1280-1284 (Pubitemid 34522777)
    • (2002) Science , vol.296 , Issue.5571 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 46
    • 77951589688 scopus 로고    scopus 로고
    • Cooperation between translating ribosomes and RNA polymerase in transcrip-tion elongation
    • Proshkin S, Rahmouni AR, Mironov A, Nudler E (2010) Cooperation between translating ribosomes and RNA polymerase in transcrip-tion elongation. Science 328: 504-508
    • (2010) Science , vol.328 , pp. 504-508
    • Proshkin, S.1    Rahmouni, A.R.2    Mironov, A.3    Nudler, E.4
  • 47
    • 2642588196 scopus 로고    scopus 로고
    • Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus
    • DOI 10.1002/prot.20054
    • Reay P, Yamasaki K, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S (2004) Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus. Proteins 56: 40-51 (Pubitemid 38720837)
    • (2004) Proteins: Structure, Function and Genetics , vol.56 , Issue.1 , pp. 40-51
    • Reay, P.1    Yamasaki, K.2    Terada, T.3    Kuramitsu, S.4    Shirouzu, M.5    Yokoyama, S.6
  • 48
    • 78649866419 scopus 로고    scopus 로고
    • Functional analysis of Thermus thermophilus transcription factor NusG
    • Sevostyanova A, Artsimovitch I (2010) Functional analysis of Thermus thermophilus transcription factor NusG. Nucleic Acids Res 38: 7432-7445
    • (2010) Nucleic Acids Res , vol.38 , pp. 7432-7445
    • Sevostyanova, A.1    Artsimovitch, I.2
  • 50
    • 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 JT, Marinkovic S, Huber R, Wahl MC (2002) Crystal structures of transcription factor NusG in light of its nucleic acid-and protein-binding activities. EMBO J21: 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
  • 51
    • 77958608570 scopus 로고    scopus 로고
    • A dual interface determines the recognition of RNA poly-merase II by RNA capping enzyme
    • Suh MH, Meyer PA, Gu M, Ye P, Zhang M, Kaplan CD, Lima CD, Fu J (2010) A dual interface determines the recognition of RNA poly-merase II by RNA capping enzyme. J Biol Chem 285: 34027-34038
    • (2010) J Biol Chem , vol.285 , pp. 34027-34038
    • Suh, M.H.1    Meyer, P.A.2    Gu, M.3    Ye, P.4    Zhang, M.5    Kaplan, C.D.6    Lima, C.D.7    Fu, J.8
  • 52
    • 0026527997 scopus 로고
    • Requirement for E. coli NusG protein in factor-dependent transcription termination
    • Sullivan SL, Gottesman ME (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
  • 53
    • 67449116330 scopus 로고    scopus 로고
    • Structural basis of transcription: Mismatch-specific fidelity mechanisms and paused RNA poly-merase II with frayed RNA
    • Sydow JF, Brueckner F, Cheung AC, Damsma GE, Dengl S, Lehmann E, Vassylyev D, Cramer P (2009) Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA poly-merase 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    Vassylyev, D.7    Cramer, P.8
  • 55
    • 30044431985 scopus 로고    scopus 로고
    • RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit
    • DOI 10.1038/nsmb1026
    • Ujvari A, Luse DS (2006) RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit. Nat Struct Mol Biol 13: 49-54 (Pubitemid 43049402)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.1 , pp. 49-54
    • Ujvari, A.1    Luse, D.S.2
  • 56
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6. Å resolution
    • DOI 10.1038/nature752
    • Vassylyev DG, Sekine S, Laptenko O, Lee J, Vassylyeva MN, 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
  • 57
    • 34447499995 scopus 로고    scopus 로고
    • Structural basis for transcription elongation by bacterial RNA polymerase
    • DOI 10.1038/nature05932, PII NATURE05932
    • Vassylyev DG, Vassylyeva MN, Perederina A, Tahirov TH, 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
  • 58
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • DOI 10.1093/emboj/17.24.7395
    • Wada T, Takagi T, Yamaguchi Y Watanabe D, Handa H (1998) Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J 17: 7395-7403 (Pubitemid 29002707)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 59
    • 0033566042 scopus 로고    scopus 로고
    • Transcription elongation factor hSPT5 stimulates mRNA capping
    • Wen Y, Shatkin AJ (1999) Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev 13: 1774-1779 (Pubitemid 29353045)
    • (1999) Genes and Development , vol.13 , Issue.14 , pp. 1774-1779
    • Wen, Y.1    Shatkin, A.J.2
  • 60
    • 8444243746 scopus 로고    scopus 로고
    • Collective motions of RNA polymerases. Analysis of core enzyme, elongation complex and holoenzyme
    • Yildirim Y Doruker P (2004) Collective motions of RNA poly-merases. Analysis of core enzyme, elongation complex and holoenzyme. J Biomol Struct Dyn 22: 267-280 (Pubitemid 39488527)
    • (2004) Journal of Biomolecular Structure and Dynamics , vol.22 , Issue.3 , pp. 267-280
    • Yildirim, Y.1    Doruker, P.2
  • 61
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution [see comments]
    • Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution [see comments]. Cell 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
  • 62
    • 66349122952 scopus 로고    scopus 로고
    • Control of transcriptional elongation and cotranscriptional histone modifi-cation by the yeast BUR kinase substrate Spt5
    • Zhou K, Kuo WH, Fillingham J, Greenblatt JF (2009) Control of transcriptional elongation and cotranscriptional histone modifi-cation by the yeast BUR kinase substrate Spt5. Proc Natl Acad Sci USA 106: 6956-6961
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6956-6961
    • Zhou, K.1    Kuo, W.H.2    Fillingham, J.3    Greenblatt, J.F.4


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