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Volumn 40, Issue 15, 2012, Pages 7442-7451

Active site opening and closure control translocation of Multisubunit RNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; NUCLEOTIDE; PYROPHOSPHATE; RNA POLYMERASE; TAGETITOXIN; UNCLASSIFIED DRUG;

EID: 84867297989     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks383     Document Type: Article
Times cited : (78)

References (44)
  • 1
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz, T. A. (1998) A mechanism for all polymerases. Nature, 391, 231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 3
    • 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. and Kornberg, R. D. (2006) Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell, 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
  • 4
    • 0027106595 scopus 로고
    • New models for the mechanism of transcription elongation and its regulation
    • Chamberlin, M. J. (1992) New models for the mechanism of transcription elongation and its regulation. Harvey Lect., 88, 1-21.
    • (1992) Harvey Lect. , vol.88 , pp. 1-21
    • Chamberlin, M.J.1
  • 7
    • 33846958387 scopus 로고    scopus 로고
    • Mechanochemical kinetics of transcription elongation
    • Bai, L., Fulbright, R. M. and Wang, M. D. (2007) Mechanochemical kinetics of transcription elongation. Phys. Rev. Lett., 98, 068103.
    • (2007) Phys. Rev. Lett. , vol.98 , pp. 068103
    • Bai, L.1    Fulbright, R.M.2    Wang, M.D.3
  • 8
    • 0032582494 scopus 로고    scopus 로고
    • Force and velocity measured for single molecules of RNA polymerase
    • Wang, M. D., Schnitzer, M. J., Yin, H., Landick, R., Gelles, J. and Block, S. M. (1998) Force and velocity measured for single molecules of RNA polymerase. Science, 282, 902-907.
    • (1998) Science , vol.282 , pp. 902-907
    • Wang, M.D.1    Schnitzer, M.J.2    Yin, H.3    Landick, R.4    Gelles, J.5    Block, S.M.6
  • 9
    • 0032584643 scopus 로고    scopus 로고
    • An integrated model of the transcription complex in elongation, termination, and editing
    • von Hippel, P. H. (1998) An integrated model of the transcription complex in elongation, termination, and editing. Science, 281, 660-665.
    • (1998) Science , vol.281 , pp. 660-665
    • Von Hippel, P.H.1
  • 10
    • 67650938441 scopus 로고    scopus 로고
    • RNA polymerase active center: The molecular engine of transcription
    • Nudler, E. (2009) RNA polymerase active center: the molecular engine of transcription. Annu. Rev. Biochem., 78, 335-361.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 335-361
    • Nudler, E.1
  • 11
    • 77953711880 scopus 로고    scopus 로고
    • Translocation by multi-subunit RNA polymerases
    • Kireeva, M., Kashlev, M. and Burton, Z. F. (2010) Translocation by multi-subunit RNA polymerases. Biochim. Biophys. Acta., 1799, 389-401.
    • (2010) Biochim. Biophys. Acta. , vol.1799 , pp. 389-401
    • Kireeva, M.1    Kashlev, M.2    Burton, Z.F.3
  • 12
    • 33747621427 scopus 로고    scopus 로고
    • Visualizing polynucleotide polymerase machines at work
    • Steitz, T. A. (2006) Visualizing polynucleotide polymerase machines at work. EMBO J., 25, 3458-3468.
    • (2006) EMBO J. , vol.25 , pp. 3458-3468
    • Steitz, T.A.1
  • 13
    • 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. and Kornberg, R. D. (2001) Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science, 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
  • 14
    • 49449102926 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation
    • Brueckner, F. and Cramer, P. (2008) Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation. Nat. Struct. Mol. Biol., 15, 811-818.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 811-818
    • Brueckner, F.1    Cramer, P.2
  • 17
    • 0029941861 scopus 로고    scopus 로고
    • A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases
    • Heikinheimo, P., Pohjanjoki, P., Helminen, A., Tasanen, M., Cooperman, B. S., Goldman, A., Baykov, A. and Lahti, R. (1996) A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases. Eur. J. Biochem., 239, 138-143.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 138-143
    • Heikinheimo, P.1    Pohjanjoki, P.2    Helminen, A.3    Tasanen, M.4    Cooperman, B.S.5    Goldman, A.6    Baykov, A.7    Lahti, R.8
  • 18
    • 0032555184 scopus 로고    scopus 로고
    • Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli
    • Brune, M., Hunter, J. L., Howell, S. A., Martin, S. R., Hazlett, T. L., Corrie, J. E. and Webb, M. R. (1998) Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli. Biochemistry, 37, 10370-10380.
    • (1998) Biochemistry , vol.37 , pp. 10370-10380
    • Brune, M.1    Hunter, J.L.2    Howell, S.A.3    Martin, S.R.4    Hazlett, T.L.5    Corrie, J.E.6    Webb, M.R.7
  • 21
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune, M., Hunter, J. L., Corrie, J. E. and Webb, M. R. (1994) Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry, 33, 8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 22
    • 25444515175 scopus 로고    scopus 로고
    • A continuous fluorescent assay for protein prenyltransferases measuring diphosphate release
    • Pais, J. E., Bowers, K. E., Stoddard, A. K. and Fierke, C. A. (2005) A continuous fluorescent assay for protein prenyltransferases measuring diphosphate release. Anal. Biochem., 345, 302-311.
    • (2005) Anal. Biochem. , vol.345 , pp. 302-311
    • Pais, J.E.1    Bowers, K.E.2    Stoddard, A.K.3    Fierke, C.A.4
  • 23
    • 34248592685 scopus 로고    scopus 로고
    • Synthesis, purification and sample experiment for fluorescent pteridine-containing DNA: Tools for studying DNA interactive systems
    • Hawkins, M. E. (2007) Synthesis, purification and sample experiment for fluorescent pteridine-containing DNA: tools for studying DNA interactive systems. Nat. Protoc., 2, 1013-1021.
    • (2007) Nat. Protoc. , vol.2 , pp. 1013-1021
    • Hawkins, M.E.1
  • 25
    • 78149234446 scopus 로고    scopus 로고
    • DNA conformational changes at the primer-template junction regulate the fidelity of replication by DNA polymerase
    • Datta, K., Johnson, N. P. and von Hippel, P. H. (2010) DNA conformational changes at the primer-template junction regulate the fidelity of replication by DNA polymerase. Proc. Natl Acad. Sci. USA, 107, 17980-17985.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17980-17985
    • Datta, K.1    Johnson, N.P.2    Von Hippel, P.H.3
  • 26
    • 78650864353 scopus 로고    scopus 로고
    • Fluorescence-based assay to measure the real-time kinetics of nucleotide incorporation during transcription elongation
    • Tang, G. Q., Anand, V. S. and Patel, S. S. (2011) Fluorescence-based assay to measure the real-time kinetics of nucleotide incorporation during transcription elongation. J. Mol. Biol., 405, 666-678.
    • (2011) J. Mol. Biol. , vol.405 , pp. 666-678
    • Tang, G.Q.1    Anand, V.S.2    Patel, S.S.3
  • 28
    • 48749102174 scopus 로고    scopus 로고
    • Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase
    • Johnson, R. S., Strausbauch, M., Cooper, R. and Register, J. K. (2008) Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase. J. Mol. Biol., 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
  • 30
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M. R. (1992) A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl Acad. Sci. USA, 89, 4884-4887.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 32
    • 80051538984 scopus 로고    scopus 로고
    • RNA transcript 30-proximal sequence affects translocation bias of RNA polymerase
    • Hein, P. P., Palangat, M. and Landick, R. (2011) RNA transcript 30-proximal sequence affects translocation bias of RNA polymerase. Biochemistry, 50, 7002-7014.
    • (2011) Biochemistry , vol.50 , pp. 7002-7014
    • Hein, P.P.1    Palangat, M.2    Landick, R.3
  • 33
    • 4644265121 scopus 로고    scopus 로고
    • Discrimination against deoxyribonucleotide substrates by bacterial RNA polymerase
    • Svetlov, V., Vassylyev, D. G. and Artsimovitch, I. (2004) Discrimination against deoxyribonucleotide substrates by bacterial RNA polymerase. J. Biol. Chem., 279, 38087-38090.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38087-38090
    • Svetlov, V.1    Vassylyev, D.G.2    Artsimovitch, I.3
  • 34
    • 77449093660 scopus 로고    scopus 로고
    • Role of the RNA polymerase trigger loop in catalysis and pausing
    • Zhang, J., Palangat, M. and Landick, R. (2010) Role of the RNA polymerase trigger loop in catalysis and pausing. Nat. Struct. Mol. Biol., 17, 99-104.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 99-104
    • Zhang, J.1    Palangat, M.2    Landick, R.3
  • 38
    • 77449145343 scopus 로고    scopus 로고
    • RNA polymerase II flexibility during translocation from normal mode analysis
    • Feig, M. and Burton, Z. F. (2010) RNA polymerase II flexibility during translocation from normal mode analysis. Proteins, 78, 434-446.
    • (2010) Proteins , vol.78 , pp. 434-446
    • Feig, M.1    Burton, Z.F.2
  • 39
    • 78049347876 scopus 로고    scopus 로고
    • RNA polymerase II with open and closed trigger loops: Active site dynamics and nucleic acid translocation
    • Feig, M. and Burton, Z. F. (2010) RNA polymerase II with open and closed trigger loops: active site dynamics and nucleic acid translocation. Biophys. J., 99, 2577-2586.
    • (2010) Biophys. J. , vol.99 , pp. 2577-2586
    • Feig, M.1    Burton, Z.F.2
  • 40
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • Yin, Y. W. and Steitz, T. A. (2004) The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell, 116, 393-404.
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, Y.W.1    Steitz, T.A.2
  • 41
    • 34547175132 scopus 로고    scopus 로고
    • Structures of phi29 DNA polymerase complexed with substrate: The mechanism of translocation in B-family polymerases
    • Berman, A. J., Kamtekar, S., Goodman, J. L., Lazaro, J. M., de Vega, M., Blanco, L., Salas, M. and Steitz, T. A. (2007) Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. EMBO J., 26, 3494-3505.
    • (2007) EMBO J. , vol.26 , pp. 3494-3505
    • Berman, A.J.1    Kamtekar, S.2    Goodman, J.L.3    Lazaro, J.M.4    Vega, M.5    Blanco, L.6    Salas, M.7    Steitz, T.A.8
  • 42
    • 73449100115 scopus 로고    scopus 로고
    • The mechanism of the translocation step in DNA replication by DNA polymerase I: A computer simulation analysis
    • Golosov, A. A., Warren, J. J., Beese, L. S. and Karplus, M. (2010) The mechanism of the translocation step in DNA replication by DNA polymerase I: a computer simulation analysis. Structure, 18, 83-93.
    • (2010) Structure , vol.18 , pp. 83-93
    • Golosov, A.A.1    Warren, J.J.2    Beese, L.S.3    Karplus, M.4
  • 43
    • 34047257841 scopus 로고    scopus 로고
    • The pyrophosphate analogue foscarnet traps the pre-translocational state of HIV-1 reverse transcriptase in a Brownian ratchet model of polymerase translocation
    • Marchand, B., Tchesnokov, E. P. and Gotte, M. (2007) The pyrophosphate analogue foscarnet traps the pre-translocational state of HIV-1 reverse transcriptase in a Brownian ratchet model of polymerase translocation. J. Biol. Chem., 282, 3337-3346.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3337-3346
    • Marchand, B.1    Tchesnokov, E.P.2    Gotte, M.3
  • 44
    • 79960134404 scopus 로고    scopus 로고
    • Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase
    • Zahn, K. E., Tchesnokov, E. P., Gotte, M. and Doublie, S. (2011) Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase. J. Biol. Chem., 286, 25246-25255.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25246-25255
    • Zahn, K.E.1    Tchesnokov, E.P.2    Gotte, M.3    Doublie, S.4


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