메뉴 건너뛰기




Volumn 16, Issue 6, 2004, Pages 955-965

Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS

Author keywords

[No Author keywords available]

Indexed keywords

DNA HYBRID; ELONGATION FACTOR; NUCLEOSIDE TRIPHOSPHATE; RNA POLYMERASE; RNA POLYMERASE II;

EID: 10944232674     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.11.040     Document Type: Article
Times cited : (355)

References (47)
  • 1
    • 0037495037 scopus 로고    scopus 로고
    • Architecture of the initiation-competent 12-subunit RNA polymerase II
    • Armache K.-J., Kettenberger H., Cramer P. Architecture of the initiation-competent 12-subunit RNA polymerase II. Proc. Natl. Acad. Sci. USA. 100:2003;6964-6968
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6964-6968
    • Armache, K.-J.1    Kettenberger, H.2    Cramer, P.3
  • 3
    • 0037832543 scopus 로고    scopus 로고
    • Complete RNA polymerase II at 4.1 Å resolution: Implications for the initiation of transcription
    • Bushnell D.A., Kornberg R.D. Complete RNA polymerase II at 4.1 Å resolution. implications for the initiation of transcription Proc. Natl. Acad. Sci. USA. 100:2003;6969-6972
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6969-6972
    • Bushnell, D.A.1    Kornberg, R.D.2
  • 4
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms
    • Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D. Structural basis of transcription. an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms Science. 303:2004;983-988
    • (2004) Science , vol.303 , pp. 983-988
    • Bushnell, D.A.1    Westover, K.D.2    Davis, R.E.3    Kornberg, R.D.4
  • 5
    • 0141992120 scopus 로고    scopus 로고
    • Binding of TFIIB to RNA polymerase II: Mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex
    • Chen H.T., Hahn S. Binding of TFIIB to RNA polymerase II. mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex Mol. Cell. 12:2003;437-447
    • (2003) Mol. Cell , vol.12 , pp. 437-447
    • Chen, H.T.1    Hahn, S.2
  • 6
    • 5444275331 scopus 로고    scopus 로고
    • Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: A model for the structure of the PIC
    • Chen H.T., Hahn S. Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex. a model for the structure of the PIC Cell. 119:2004;169-180
    • (2004) Cell , vol.119 , pp. 169-180
    • Chen, H.T.1    Hahn, S.2
  • 8
    • 0036690340 scopus 로고    scopus 로고
    • Structure of yeast RNA polymerase II in solution: Implications for enzyme regulation and interaction with promoter DNA
    • Craighead J.L., Chang W.H., Asturias F.J. Structure of yeast RNA polymerase II in solution. implications for enzyme regulation and interaction with promoter DNA Struct. Fold. Des. 10:2002;1117-1125
    • (2002) Struct. Fold. Des. , vol.10 , pp. 1117-1125
    • Craighead, J.L.1    Chang, W.H.2    Asturias, F.J.3
  • 9
    • 1942535198 scopus 로고    scopus 로고
    • RNA polymerase II structure: From core to functional complexes
    • a
    • Cramer P. RNA polymerase II structure. from core to functional complexes Curr. Opin. Genet. Dev. 14:2004;218-226. a
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 218-226
    • Cramer, P.1
  • 10
    • 1242273889 scopus 로고    scopus 로고
    • Structure and function of RNA polymerase II
    • b
    • Cramer P. Structure and function of RNA polymerase II. Adv. Protein Chem. 67:2004;1-42. b
    • (2004) Adv. Protein Chem. , vol.67 , pp. 1-42
    • Cramer, P.1
  • 12
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P., Bushnell D.A., Kornberg R.D. Structural basis of transcription. RNA polymerase II at 2.8 angstrom resolution Science. 292:2001;1863-1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 13
    • 0037073062 scopus 로고    scopus 로고
    • The many conformational states of RNA polymerase elongation complexes and their roles in the regulation of transcription
    • Erie D.A. The many conformational states of RNA polymerase elongation complexes and their roles in the regulation of transcription. Biochim. Biophys. Acta. 1577:2002;224-239
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 224-239
    • Erie, D.A.1
  • 14
    • 0037073048 scopus 로고    scopus 로고
    • Promoting elongation with transcript cleavage stimulatory factors
    • Fish R.N., Kane C.M. Promoting elongation with transcript cleavage stimulatory factors. Biochim. Biophys. Acta. 1577:2002;287-307
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 287-307
    • Fish, R.N.1    Kane, C.M.2
  • 15
    • 1642540256 scopus 로고    scopus 로고
    • Photo-cross-linking of a purified preinitiation complex reveals central roles for the RNA polymerase II mobile clamp and TFIIE in initiation mechanisms
    • Forget D., Langelier M.F., Therien C., Trinh V., Coulombe B. Photo-cross-linking of a purified preinitiation complex reveals central roles for the RNA polymerase II mobile clamp and TFIIE in initiation mechanisms. Mol. Cell. Biol. 24:2004;1122-1131
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1122-1131
    • Forget, D.1    Langelier, M.F.2    Therien, C.3    Trinh, V.4    Coulombe, B.5
  • 16
    • 0037073076 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: Structure-function relationship
    • Gnatt A. Elongation by RNA polymerase II. structure-function relationship Biochim. Biophys. Acta. 1577:2002;175-190
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 175-190
    • Gnatt, A.1
  • 17
    • 0030667144 scopus 로고    scopus 로고
    • Formation and crystallization of yeast RNA polymerase II elongation complexes
    • Gnatt A., Fu J., Kornberg R.D. Formation and crystallization of yeast RNA polymerase II elongation complexes. J. Biol. Chem. 272:1997;30799-30805
    • (1997) J. Biol. Chem. , vol.272 , pp. 30799-30805
    • Gnatt, A.1    Fu, J.2    Kornberg, R.D.3
  • 18
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 a resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription. an RNA polymerase II elongation complex at 3.3 A resolution Science. 292:2001;1876-1882
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 19
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • Kettenberger H., Armache K.-J., Cramer P. Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell. 114:2003;347-357
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 20
    • 0034717308 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent promoter melting by transcription factor IIH
    • Kim T.K., Ebright R.H., Reinberg D. Mechanism of ATP-dependent promoter melting by transcription factor IIH. Science. 288:2000;1418-1422
    • (2000) Science , vol.288 , pp. 1418-1422
    • Kim, T.K.1    Ebright, R.H.2    Reinberg, D.3
  • 21
    • 0034595503 scopus 로고    scopus 로고
    • Overextended RNA:DNA hybrid as a negative regulator of RNA polymerase II processivity
    • a
    • Kireeva M.L., Komissarova N., Kashlev M. Overextended RNA:DNA hybrid as a negative regulator of RNA polymerase II processivity. J. Mol. Biol. 299:2000;325-335. a
    • (2000) J. Mol. Biol. , vol.299 , pp. 325-335
    • Kireeva, M.L.1    Komissarova, N.2    Kashlev, M.3
  • 22
    • 0034051171 scopus 로고    scopus 로고
    • The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex
    • b
    • Kireeva M.L., Komissarova N., Waugh D.S., Kashlev M. The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex. J. Biol. Chem. 275:2000;6530-6536. b
    • (2000) J. Biol. Chem. , vol.275 , pp. 6530-6536
    • Kireeva, M.L.1    Komissarova, N.2    Waugh, D.S.3    Kashlev, M.4
  • 24
    • 1642417611 scopus 로고    scopus 로고
    • Active-site dynamics in RNA polymerases
    • Landick R. Active-site dynamics in RNA polymerases. Cell. 116:2004;351-353
    • (2004) Cell , vol.116 , pp. 351-353
    • Landick, R.1
  • 25
    • 0348111451 scopus 로고    scopus 로고
    • An extended winged helix domain in general transcription factor E/IIEα
    • Meinhart A., Blobel J., Cramer P. An extended winged helix domain in general transcription factor E/IIEα J. Biol. Chem. 278:2003;48267-48274
    • (2003) J. Biol. Chem. , vol.278 , pp. 48267-48274
    • Meinhart, A.1    Blobel, J.2    Cramer, P.3
  • 26
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., Masuda S., Campbell E.A., Muzzin O., Darst S.A. Structural basis of transcription initiation. an RNA polymerase holoenzyme-DNA complex Science. 296:2002;1285-1290
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 27
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • Naryshkin N., Revyakin A., Kim Y., Mekler V., Ebright R.H. Structural organization of the RNA polymerase-promoter open complex. Cell. 101:2000;601-611
    • (2000) Cell , vol.101 , pp. 601-611
    • Naryshkin, N.1    Revyakin, A.2    Kim, Y.3    Mekler, V.4    Ebright, R.H.5
  • 28
    • 0033597378 scopus 로고    scopus 로고
    • Transcription elongation: Structural basis and mechanisms
    • Nudler E. Transcription elongation. structural basis and mechanisms J. Mol. Biol. 288:1999;1-12
    • (1999) J. Mol. Biol. , vol.288 , pp. 1-12
    • Nudler, E.1
  • 29
    • 0029818631 scopus 로고    scopus 로고
    • Transcription processivity: Protein-DNA interactions holding together the elongation complex
    • Nudler E., Avetissova E., Markovtsov V., Goldfarb A. Transcription processivity. Protein-DNA interactions holding together the elongation complex Science. 273:1996;211-217
    • (1996) Science , vol.273 , pp. 211-217
    • Nudler, E.1    Avetissova, E.2    Markovtsov, V.3    Goldfarb, A.4
  • 30
    • 0032541021 scopus 로고    scopus 로고
    • Spatial organization of transcription elongation complex in Escherichia coli
    • Nudler E., Gusarov I., Avetissova E., Kozlov M., Goldfarb A. Spatial organization of transcription elongation complex in Escherichia coli. Science. 281:1998;424-428
    • (1998) Science , vol.281 , pp. 424-428
    • Nudler, E.1    Gusarov, I.2    Avetissova, E.3    Kozlov, M.4    Goldfarb, A.5
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth Enzym. 276:1996;307-326
    • (1996) Meth Enzym , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0032087891 scopus 로고    scopus 로고
    • Transcriptional pausing at +62 of HIV-1 nascent RNA modulates formation of the TAR RNA structure
    • Palangat M., Meier T.I., Keene R.G., Landick R. Transcriptional pausing at +62 of HIV-1 nascent RNA modulates formation of the TAR RNA structure. Mol. Cell. 1:1998;1033-1042
    • (1998) Mol. Cell , vol.1 , pp. 1033-1042
    • Palangat, M.1    Meier, T.I.2    Keene, R.G.3    Landick, R.4
  • 33
    • 3343017588 scopus 로고    scopus 로고
    • Downstream DNA selectively affects a paused conformation of human RNA polymerase II
    • Palangat M., Hittinger C.T., Landick R. Downstream DNA selectively affects a paused conformation of human RNA polymerase II. J. Mol. Biol. 341:2004;429-442
    • (2004) J. Mol. Biol. , vol.341 , pp. 429-442
    • Palangat, M.1    Hittinger, C.T.2    Landick, R.3
  • 36
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • Sosunov V., Sosunova E., Mustaev A., Bass I., Nikiforov V., Goldfarb A. Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase. EMBO J. 22:2003;2234-2244
    • (2003) EMBO J. , vol.22 , pp. 2234-2244
    • Sosunov, V.1    Sosunova, E.2    Mustaev, A.3    Bass, I.4    Nikiforov, V.5    Goldfarb, A.6
  • 37
    • 1342302799 scopus 로고    scopus 로고
    • The structural basis of the transition from initiation to elongation phases of transcription, as well as translocation and strand separation, by T7 RNA polymerase
    • Steitz T.A. The structural basis of the transition from initiation to elongation phases of transcription, as well as translocation and strand separation, by T7 RNA polymerase. Curr. Opin. Struct. Biol. 14:2004;4-9
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 4-9
    • Steitz, T.A.1
  • 38
    • 4644265121 scopus 로고    scopus 로고
    • Discrimination against deoxyribonucleotide substrates by bacterial RNA polymerase
    • Svetlov V., Vassylyev D.G., Artsimovitch I. Discrimination against deoxyribonucleotide substrates by bacterial RNA polymerase. J. Biol. Chem. 279:2004;38087-38090
    • (2004) J. Biol. Chem. , vol.279 , pp. 38087-38090
    • Svetlov, V.1    Vassylyev, D.G.2    Artsimovitch, I.3
  • 41
    • 0036753399 scopus 로고    scopus 로고
    • A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription
    • Werner F., Weinzierl R.O. A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription. Mol. Cell. 10:2002;635-646
    • (2002) Mol. Cell , vol.10 , pp. 635-646
    • Werner, F.1    Weinzierl, R.O.2
  • 42
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: Separation of RNA from DNA by RNA polymerase II
    • a
    • Westover K.D., Bushnell D.A., Kornberg R.D. Structural basis of transcription. separation of RNA from DNA by RNA polymerase II Science. 303:2004;1014-1016. a
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 43
    • 8344234112 scopus 로고    scopus 로고
    • Structural basis of transcription: Nucleotide selection by rotation in the RNA polymerase II active center
    • b
    • Westover K.D., Bushnell D.A., Kornberg R.D. Structural basis of transcription. nucleotide selection by rotation in the RNA polymerase II active center Cell. 119:2004;481-489. b
    • (2004) Cell , vol.119 , pp. 481-489
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 44
    • 0034006399 scopus 로고    scopus 로고
    • Transcription elongation factor SII
    • Wind M., Reines D. Transcription elongation factor SII. Bioessays. 22:2000;327-336
    • (2000) Bioessays , vol.22 , pp. 327-336
    • Wind, M.1    Reines, D.2
  • 45
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science. 298:2002;1387-1395
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 46
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in t7 RNA polymerase
    • Yin Y.W., Steitz T.A. The structural mechanism of translocation and helicase activity in t7 RNA polymerase. Cell. 116:2004;393-404
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, Y.W.1    Steitz, T.A.2
  • 47
    • 4444228491 scopus 로고    scopus 로고
    • Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism
    • Zhang C., Burton Z.F. Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism. J. Mol. Biol. 342:2004;1085-1099
    • (2004) J. Mol. Biol. , vol.342 , pp. 1085-1099
    • Zhang, C.1    Burton, Z.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.