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Volumn 1829, Issue 2, 2013, Pages 187-198

The RNA polymerase bridge helix YFI motif in catalysis, fidelity and translocation

Author keywords

Bridge helix; Pausing; RNA polymerase; Termination; Transcriptional fidelity; Translocation

Indexed keywords

GLYCINE; RNA POLYMERASE;

EID: 84872407990     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2012.11.005     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 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
  • 2
    • 67650938441 scopus 로고    scopus 로고
    • RNA polymerase active center: the molecular engine of transcription
    • Nudler E. RNA polymerase active center: the molecular engine of transcription. Annu. Rev. Biochem. 2009, 78:335-361.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 335-361
    • Nudler, E.1
  • 4
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis
    • Wang D., Bushnell D.A., Westover K.D., Kaplan C.D., Kornberg R.D. Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 2006, 127:941-954.
    • (2006) Cell , vol.127 , pp. 941-954
    • Wang, D.1    Bushnell, D.A.2    Westover, K.D.3    Kaplan, C.D.4    Kornberg, R.D.5
  • 6
    • 78049347876 scopus 로고    scopus 로고
    • RNA polymerase II with open and closed trigger loops: active site dynamics and nucleic acid translocation
    • Feig M., Burton Z.F. RNA polymerase II with open and closed trigger loops: active site dynamics and nucleic acid translocation. Biophys. J. 2010, 99:2577-2586.
    • (2010) Biophys. J. , vol.99 , pp. 2577-2586
    • Feig, M.1    Burton, Z.F.2
  • 7
    • 77449145343 scopus 로고    scopus 로고
    • RNA polymerase II flexibility during translocation from normal mode analysis
    • Feig M., Burton Z.F. RNA polymerase II flexibility during translocation from normal mode analysis. Proteins 2010, 78:434-446.
    • (2010) Proteins , vol.78 , pp. 434-446
    • Feig, M.1    Burton, Z.F.2
  • 8
    • 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 2001, 292:1876-1882.
    • (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
  • 10
    • 57249108333 scopus 로고    scopus 로고
    • Bridge helix and trigger loop perturbations generate superactive RNA polymerases
    • Tan L., Wiesler S., Trzaska D., Carney H.C., Weinzierl R.O. Bridge helix and trigger loop perturbations generate superactive RNA polymerases. J. Biol. 2008, 7:40.
    • (2008) J. Biol. , vol.7 , pp. 40
    • Tan, L.1    Wiesler, S.2    Trzaska, D.3    Carney, H.C.4    Weinzierl, R.O.5
  • 11
    • 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
  • 14
    • 84858225724 scopus 로고    scopus 로고
    • The Bridge Helix of RNA polymerase acts as a central nanomechanical switchboard for coordinating catalysis and substrate movement
    • Weinzierl R.O. The Bridge Helix of RNA polymerase acts as a central nanomechanical switchboard for coordinating catalysis and substrate movement. Archaea 2011, 2011:608385.
    • (2011) Archaea , vol.2011 , pp. 608385
    • Weinzierl, R.O.1
  • 15
    • 84869783692 scopus 로고    scopus 로고
    • RNA polymerase stalls in a post-translocated register and can hyper-translocate
    • Nedialkov Y.A., Nudler E., Burton Z.F. RNA polymerase stalls in a post-translocated register and can hyper-translocate. Transcription 2012, 3:260-269.
    • (2012) Transcription , vol.3 , pp. 260-269
    • Nedialkov, Y.A.1    Nudler, E.2    Burton, Z.F.3
  • 17
    • 0142147268 scopus 로고    scopus 로고
    • A new class of bacterial RNA polymerase inhibitor affects nucleotide addition
    • Artsimovitch I., Chu C., Lynch A.S., Landick R. A new class of bacterial RNA polymerase inhibitor affects nucleotide addition. Science 2003, 302:650-654.
    • (2003) Science , vol.302 , pp. 650-654
    • Artsimovitch, I.1    Chu, C.2    Lynch, A.S.3    Landick, R.4
  • 19
    • 0034051171 scopus 로고    scopus 로고
    • The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex
    • 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. 2000, 275:6530-6536.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6530-6536
    • Kireeva, M.L.1    Komissarova, N.2    Waugh, D.S.3    Kashlev, M.4
  • 21
    • 67849124180 scopus 로고    scopus 로고
    • Millisecond phase kinetic analysis of elongation catalyzed by human, yeast, and Escherichia coli RNA polymerase
    • Kireeva M., Nedialkov Y.A., Gong X.Q., Zhang C., Xiong Y., Moon W., Burton Z.F., Kashlev M. Millisecond phase kinetic analysis of elongation catalyzed by human, yeast, and Escherichia coli RNA polymerase. Methods 2009, 48:333-345.
    • (2009) Methods , vol.48 , pp. 333-345
    • Kireeva, M.1    Nedialkov, Y.A.2    Gong, X.Q.3    Zhang, C.4    Xiong, Y.5    Moon, W.6    Burton, Z.F.7    Kashlev, M.8
  • 25
    • 0033120034 scopus 로고    scopus 로고
    • The mechanism of intrinsic transcription termination
    • Gusarov I., Nudler E. The mechanism of intrinsic transcription termination. Mol. Cell 1999, 3:495-504.
    • (1999) Mol. Cell , vol.3 , pp. 495-504
    • Gusarov, I.1    Nudler, E.2
  • 26
    • 0035958552 scopus 로고    scopus 로고
    • Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation
    • Foster J.E., Holmes S.F., Erie D.A. Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation. Cell 2001, 106:243-252.
    • (2001) Cell , vol.106 , pp. 243-252
    • Foster, J.E.1    Holmes, S.F.2    Erie, D.A.3
  • 29
    • 79955027964 scopus 로고    scopus 로고
    • Templated nucleoside triphosphate binding to a noncatalytic site on RNA polymerase regulates transcription
    • Kennedy S.R., Erie D.A. Templated nucleoside triphosphate binding to a noncatalytic site on RNA polymerase regulates transcription. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:6079-6084.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6079-6084
    • Kennedy, S.R.1    Erie, D.A.2
  • 31
    • 80053378346 scopus 로고    scopus 로고
    • Rapid pyrophosphate release from transcriptional elongation complexes appears to be coupled to a nucleotide-induced conformational change in E. coli core polymerase
    • Johnson R.S., Strausbauch M., Carraway J.K. Rapid pyrophosphate release from transcriptional elongation complexes appears to be coupled to a nucleotide-induced conformational change in E. coli core polymerase. J. Mol. Biol. 2011, 412:849-861.
    • (2011) J. Mol. Biol. , vol.412 , pp. 849-861
    • Johnson, R.S.1    Strausbauch, M.2    Carraway, J.K.3
  • 32
    • 48749102174 scopus 로고    scopus 로고
    • Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase
    • Johnson R.S., Strausbauch M., Cooper R., Register J.K. Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase. J. Mol. Biol. 2008, 381:1106-1113.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1106-1113
    • Johnson, R.S.1    Strausbauch, M.2    Cooper, R.3    Register, J.K.4
  • 33
    • 33745808766 scopus 로고    scopus 로고
    • Kinetic investigation of Escherichia coli RNA polymerase mutants that influence nucleotide discrimination and transcription fidelity
    • Holmes S.F., Santangelo T.J., Cunningham C.K., Roberts J.W., Erie D.A. Kinetic investigation of Escherichia coli RNA polymerase mutants that influence nucleotide discrimination and transcription fidelity. J. Biol. Chem. 2006, 281:18677-18683.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18677-18683
    • Holmes, S.F.1    Santangelo, T.J.2    Cunningham, C.K.3    Roberts, J.W.4    Erie, D.A.5
  • 34
    • 80051538984 scopus 로고    scopus 로고
    • RNA transcript 3'-proximal sequence affects translocation bias of RNA polymerase
    • Hein P.P., Palangat M., Landick R. RNA transcript 3'-proximal sequence affects translocation bias of RNA polymerase. Biochemistry 2011, 50:7002-7014.
    • (2011) Biochemistry , vol.50 , pp. 7002-7014
    • Hein, P.P.1    Palangat, M.2    Landick, R.3
  • 35
    • 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
  • 36
    • 77953280325 scopus 로고    scopus 로고
    • Nanomechanical constraints acting on the catalytic site of cellular RNA polymerases
    • Weinzierl R.O. Nanomechanical constraints acting on the catalytic site of cellular RNA polymerases. Biochem. Soc. Trans. 2011, 38:428-432.
    • (2011) Biochem. Soc. Trans. , vol.38 , pp. 428-432
    • Weinzierl, R.O.1
  • 38
    • 49449102926 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation
    • Brueckner F., Cramer P. Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation. Nat. Struct. Mol. Biol. 2008, 15:811-818.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 811-818
    • Brueckner, F.1    Cramer, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.