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Volumn 18, Issue 4, 2005, Pages 461-470

Dynamic error correction and regulation of downstream bubble opening by human RNA polymerase II

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMANITIN; NUCLEOTIDE DERIVATIVE; RNA POLYMERASE II;

EID: 18944368782     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.04.011     Document Type: Article
Times cited : (53)

References (33)
  • 4
    • 10644237908 scopus 로고    scopus 로고
    • Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center
    • N.N. Batada, K.D. Westover, D.A. Bushnell, M. Levitt, and R.D. Kornberg Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center Proc. Natl. Acad. Sci. USA 101 2004 17361 17364
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17361-17364
    • Batada, N.N.1    Westover, K.D.2    Bushnell, D.A.3    Levitt, M.4    Kornberg, R.D.5
  • 5
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 a resolution
    • D.A. Bushnell, P. Cramer, and R.D. Kornberg Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution Proc. Natl. Acad. Sci. USA 99 2002 1218 1222
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 6
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • P. Cramer, D.A. Bushnell, and R.D. Kornberg 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
  • 7
    • 1942456697 scopus 로고    scopus 로고
    • Recent advances in the development and application of implicit solvent models in biomolecule simulations
    • M. Feig, and C.L. Brooks 3rd. Recent advances in the development and application of implicit solvent models in biomolecule simulations Curr. Opin. Struct. Biol. 14 2004 217 224
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 217-224
    • Feig, M.1    Brooks III, C.L.2
  • 8
    • 0035958552 scopus 로고    scopus 로고
    • Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation
    • J.E. Foster, S.F. Holmes, and D.A. Erie Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation Cell 106 2001 243 252
    • (2001) Cell , vol.106 , pp. 243-252
    • Foster, J.E.1    Holmes, S.F.2    Erie, D.A.3
  • 9
    • 0037073076 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: Structure-function relationship
    • A. Gnatt 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
  • 10
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 a resolution
    • A.L. Gnatt, P. Cramer, J. Fu, D.A. Bushnell, and R.D. Kornberg 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
  • 11
    • 2442461170 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): Kinetic, thermodynamic, and structural analysis of ribonucleotide selection
    • D.W. Gohara, J.J. Arnold, and C.E. Cameron Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection Biochemistry 43 2004 5149 5158
    • (2004) Biochemistry , vol.43 , pp. 5149-5158
    • Gohara, D.W.1    Arnold, J.J.2    Cameron, C.E.3
  • 12
    • 3042595545 scopus 로고    scopus 로고
    • Alpha-amanitin blocks translocation by human RNA polymerase II
    • X.Q. Gong, Y.A. Nedialkov, and Z.F. Burton Alpha-amanitin blocks translocation by human RNA polymerase II J. Biol. Chem. 279 2004 27422 27427
    • (2004) J. Biol. Chem. , vol.279 , pp. 27422-27427
    • Gong, X.Q.1    Nedialkov, Y.A.2    Burton, Z.F.3
  • 13
    • 0041315524 scopus 로고    scopus 로고
    • Downstream DNA sequence effects on transcription elongation. Allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion
    • S.F. Holmes, and D.A. Erie Downstream DNA sequence effects on transcription elongation. Allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion J. Biol. Chem. 278 2003 35597 35608
    • (2003) J. Biol. Chem. , vol.278 , pp. 35597-35608
    • Holmes, S.F.1    Erie, D.A.2
  • 14
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • M. Karplus, and J.A. McCammon Molecular dynamics simulations of biomolecules Nat. Struct. Biol. 9 2002 646 652
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 15
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • H. Kettenberger, K.J. Armache, and P. Cramer Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS Mol. Cell 16 2004 955 965
    • (2004) Mol. Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 16
    • 1642417611 scopus 로고    scopus 로고
    • Active-site dynamics in RNA polymerases
    • R. Landick Active-site dynamics in RNA polymerases Cell 116 2004 351 353
    • (2004) Cell , vol.116 , pp. 351-353
    • Landick, R.1
  • 19
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • S.S. Patel, I. Wong, and K.A. Johnson Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant Biochemistry 30 1991 511 525
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 20
    • 0023835505 scopus 로고
    • A high-efficiency HeLa cell nuclear transcription extract
    • D.J. Shapiro, P.A. Sharp, W.W. Wahli, and M.J. Keller A high-efficiency HeLa cell nuclear transcription extract DNA 7 1988 47 55
    • (1988) DNA , vol.7 , pp. 47-55
    • Shapiro, D.J.1    Sharp, P.A.2    Wahli, W.W.3    Keller, M.J.4
  • 21
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • V. Sosunov, E. Sosunova, A. Mustaev, I. Bass, V. Nikiforov, and A. Goldfarb 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
  • 22
    • 0347586799 scopus 로고    scopus 로고
    • On models and methods for studying polymerase translocation
    • R. Sousa On models and methods for studying polymerase translocation Methods Enzymol. 371 2003 3 13
    • (2003) Methods Enzymol. , vol.371 , pp. 3-13
    • Sousa, R.1
  • 26
    • 0028518550 scopus 로고
    • Importance of codon preference for production of human RAP74 and reconstitution of the RAP30/74 complex
    • B.Q. Wang, L. Lei, and Z.F. Burton Importance of codon preference for production of human RAP74 and reconstitution of the RAP30/74 complex Protein Expr. Purif. 5 1994 476 485
    • (1994) Protein Expr. Purif. , vol.5 , pp. 476-485
    • Wang, B.Q.1    Lei, L.2    Burton, Z.F.3
  • 27
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: Separation of RNA from DNA by RNA polymerase II
    • K.D. Westover, D.A. Bushnell, and R.D. Kornberg Structural basis of transcription: separation of RNA from DNA by RNA polymerase II Science 303 2004 1014 1016
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 28
    • 8344234112 scopus 로고    scopus 로고
    • Structural basis of transcription: Nucleotide selection by rotation in the RNA polymerase II active center
    • K.D. Westover, D.A. Bushnell, and R.D. Kornberg Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center Cell 119 2004 481 489
    • (2004) Cell , vol.119 , pp. 481-489
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 29
    • 0026026192 scopus 로고
    • An induced-fit kinetic mechanism for DNA replication fidelity: Direct measurement by single-turnover kinetics
    • I. Wong, S.S. Patel, and K.A. Johnson An induced-fit kinetic mechanism for DNA replication fidelity: direct measurement by single-turnover kinetics Biochemistry 30 1991 526 537
    • (1991) Biochemistry , vol.30 , pp. 526-537
    • Wong, I.1    Patel, S.S.2    Johnson, K.A.3
  • 30
    • 4444228491 scopus 로고    scopus 로고
    • Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism
    • C. Zhang, and Z.F. Burton 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
  • 31
    • 0346749472 scopus 로고    scopus 로고
    • Combinatorial control of human RNA polymerase II (RNAP II) pausing and transcript cleavage by transcription factor IIF, hepatitis δ antigen, and stimulatory factor II
    • C. Zhang, H. Yan, and Z.F. Burton Combinatorial control of human RNA polymerase II (RNAP II) pausing and transcript cleavage by transcription factor IIF, hepatitis δ antigen, and stimulatory factor II J. Biol. Chem. 278 2003 50101 50111
    • (2003) J. Biol. Chem. , vol.278 , pp. 50101-50111
    • Zhang, C.1    Yan, H.2    Burton, Z.F.3
  • 32
    • 17644384843 scopus 로고    scopus 로고
    • Human RNA polymerase II elongation in slow motion: Role of the TFIIF RAP74 α1 helix in NTP-driven translocation
    • C. Zhang, K.L. Zobeck, and Z. Burton Human RNA polymerase II elongation in slow motion: role of the TFIIF RAP74 α1 helix in NTP-driven translocation Mol. Cell. Biol. 25 2005 3583 3595
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3583-3595
    • Zhang, C.1    Zobeck, K.L.2    Burton, Z.3
  • 33
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 a resolution
    • G. Zhang, E.A. Campbell, L. Minakhin, C. Richter, K. Severinov, and S.A. Darst Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution Cell 98 1999 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.