메뉴 건너뛰기




Volumn 9, Issue 4, 2013, Pages

A Two-State Model for the Dynamics of the Pyrophosphate Ion Release in Bacterial RNA Polymerase

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR DYNAMICS; RNA;

EID: 84876924192     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003020     Document Type: Article
Times cited : (48)

References (56)
  • 1
    • 70249104647 scopus 로고    scopus 로고
    • Defining mechanisms that regulate RNA polymerase II transcription in vivo
    • Fuda NJ, Ardehali MB, Lis JT, (2009) Defining mechanisms that regulate RNA polymerase II transcription in vivo. Nature 461: 186-192.
    • (2009) Nature , vol.461 , pp. 186-192
    • Fuda, N.J.1    Ardehali, M.B.2    Lis, J.T.3
  • 2
    • 34548801789 scopus 로고    scopus 로고
    • The molecular basis of eukaryotic transcription
    • Kornberg RD, (2007) The molecular basis of eukaryotic transcription. Proc Natl Acad Sci USA 104: 12955-12961.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12955-12961
    • Kornberg, R.D.1
  • 3
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis
    • Wang D, Bushnell DA, Westover KD, Kaplan CD, Kornberg RD, (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
    • 0034724953 scopus 로고    scopus 로고
    • Architecture of RNA polymerase II and implications for the transcription mechanism
    • Cramer P, Bushnell DA, Fu J, Gnatt AL, Maier-Davis B, et al. (2000) Architecture of RNA polymerase II and implications for the transcription mechanism. Science 288: 640-649.
    • (2000) Science , vol.288 , pp. 640-649
    • Cramer, P.1    Bushnell, D.A.2    Fu, J.3    Gnatt, A.L.4    Maier-Davis, B.5
  • 5
    • 78650310283 scopus 로고    scopus 로고
    • Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein
    • Tagami S, Sekine S, Kumarevel T, Hino N, Murayama Y, et al. (2010) Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein. Nature 468: 978-982.
    • (2010) Nature , vol.468 , pp. 978-982
    • Tagami, S.1    Sekine, S.2    Kumarevel, T.3    Hino, N.4    Murayama, Y.5
  • 8
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
    • Vassylyev DG, Sekine S, Laptenko O, Lee J, Vassylyeva MN, et al. (2002) Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution. Nature 417: 712-719.
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1    Sekine, S.2    Laptenko, O.3    Lee, J.4    Vassylyeva, M.N.5
  • 9
    • 84862666457 scopus 로고    scopus 로고
    • A Movie of RNA Polymerase II Transcription
    • Cheung A, Cramer P, (2012) A Movie of RNA Polymerase II Transcription. Cell 149: 1431-1437.
    • (2012) Cell , vol.149 , pp. 1431-1437
    • Cheung, A.1    Cramer, P.2
  • 10
    • 70549111391 scopus 로고    scopus 로고
    • RNA polymerase fidelity and transcriptional proofreading
    • Sydow JF, Cramer P, (2009) RNA polymerase fidelity and transcriptional proofreading. Curr Opin Struc Biol 19: 732-739.
    • (2009) Curr Opin Struc Biol , vol.19 , pp. 732-739
    • Sydow, J.F.1    Cramer, P.2
  • 11
    • 70549108206 scopus 로고    scopus 로고
    • Macromolecular micromovements: how RNA polymerase translocates
    • Svetlov V, Nudler E, (2009) Macromolecular micromovements: how RNA polymerase translocates. Curr Opin Struc Biol 19: 701-707.
    • (2009) Curr Opin Struc Biol , vol.19 , pp. 701-707
    • Svetlov, V.1    Nudler, E.2
  • 12
    • 67049154068 scopus 로고    scopus 로고
    • Transcriptional pausing without backtracking
    • Landick R, (2009) Transcriptional pausing without backtracking. Proc Natl Acad Sci USA 106: 8797-8798.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8797-8798
    • Landick, R.1
  • 13
    • 66549126163 scopus 로고    scopus 로고
    • A movie of the RNA polymerase nucleotide addition cycle
    • Brueckner F, Ortiz J, Cramer P, (2009) A movie of the RNA polymerase nucleotide addition cycle. Curr Opin Struc Biol 19: 294-299.
    • (2009) Curr Opin Struc Biol , vol.19 , pp. 294-299
    • Brueckner, F.1    Ortiz, J.2    Cramer, P.3
  • 15
    • 84860131275 scopus 로고    scopus 로고
    • Efficient reconstitution of transcription elongation complexes for single-molecule studies of eukaryotic RNA polymerase II
    • Palangat M, Larson MH, Hu X, Gnatt A, Block SM, et al. (2012) Efficient reconstitution of transcription elongation complexes for single-molecule studies of eukaryotic RNA polymerase II. Transcription 3: 146-153.
    • (2012) Transcription , vol.3 , pp. 146-153
    • Palangat, M.1    Larson, M.H.2    Hu, X.3    Gnatt, A.4    Block, S.M.5
  • 16
    • 84860211901 scopus 로고    scopus 로고
    • Trigger loop dynamics mediate the balance between the transcriptional fidelity and speed of RNA polymerase II
    • Larson MH, Zhou J, Kaplan CD, Palangat M, Kornberg RD, et al. (2012) Trigger loop dynamics mediate the balance between the transcriptional fidelity and speed of RNA polymerase II. Proc Natl Acad Sci USA 109: 6555-6560.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 6555-6560
    • Larson, M.H.1    Zhou, J.2    Kaplan, C.D.3    Palangat, M.4    Kornberg, R.D.5
  • 17
    • 77957678214 scopus 로고    scopus 로고
    • RNA polymerase II trigger loop residues stabilize and position the incoming nucleotide triphosphate in transcription
    • Huang X, Wang D, Weiss DR, Bushnell DA, Kornberg RD, et al. (2010) RNA polymerase II trigger loop residues stabilize and position the incoming nucleotide triphosphate in transcription. Proc Natl Acad Sci USA 107: 15745-15750.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15745-15750
    • Huang, X.1    Wang, D.2    Weiss, D.R.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 18
    • 84860111277 scopus 로고    scopus 로고
    • Dissection of Pol II Trigger Loop Function and Pol II Activity-Dependent Control of Start Site Selection In Vivo
    • Kaplan CD, Jin H, Zhang IL, Belyanin A, (2012) Dissection of Pol II Trigger Loop Function and Pol II Activity-Dependent Control of Start Site Selection In Vivo. PLoS Genet 8: e1002627.
    • (2012) PLoS Genet , vol.8
    • Kaplan, C.D.1    Jin, H.2    Zhang, I.L.3    Belyanin, A.4
  • 19
    • 84872395984 scopus 로고    scopus 로고
    • Basic mechanisms of RNA polymerase II activity and alteration of gene expression in Saccharomyces cerevisiae
    • Kaplan CD, (2012) Basic mechanisms of RNA polymerase II activity and alteration of gene expression in Saccharomyces cerevisiae. Biochimica et Biophysica Acta (BBA)- Gene Regulatory Mechanisms 1829: 39-54.
    • (2012) Biochimica Et Biophysica Acta (BBA) - Gene Regulatory Mechanisms , vol.1829 , pp. 39-54
    • Kaplan, C.D.1
  • 20
    • 77449093660 scopus 로고    scopus 로고
    • Role of the RNA polymerase trigger loop in catalysis and pausing
    • Zhang J, Palangat M, Landick R, (2009) Role of the RNA polymerase trigger loop in catalysis and pausing. Nat Struct Mol Biol 17: 99-104.
    • (2009) Nat Struct Mol Biol , vol.17 , pp. 99-104
    • Zhang, J.1    Palangat, M.2    Landick, R.3
  • 21
    • 44449103640 scopus 로고    scopus 로고
    • The RNA Polymerase II Trigger Loop Functions in Substrate Selection and Is Directly Targeted by a-Amanitin
    • Kaplan CD, Larsson KM, Kornberg RD, (2008) The RNA Polymerase II Trigger Loop Functions in Substrate Selection and Is Directly Targeted by a-Amanitin. Mol Cell 30: 547-556.
    • (2008) Mol Cell , vol.30 , pp. 547-556
    • Kaplan, C.D.1    Larsson, K.M.2    Kornberg, R.D.3
  • 22
    • 77954655593 scopus 로고    scopus 로고
    • Central role of the RNA polymerase trigger loop in intrinsic RNA hydrolysis
    • Yuzenkova Y, Zenkin N, (2010) Central role of the RNA polymerase trigger loop in intrinsic RNA hydrolysis. Proc Natl Acad Sci USA 107: 10878-10883.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10878-10883
    • Yuzenkova, Y.1    Zenkin, N.2
  • 23
    • 84870983295 scopus 로고    scopus 로고
    • Molecular dynamics and mutational analysis of the catalytic and translocation cycle of RNA polymerase
    • Kireeva ML, Opron K, Seibold SA, Domecq C, Cukier RI, et al. (2012) Molecular dynamics and mutational analysis of the catalytic and translocation cycle of RNA polymerase. BMC Biophysics 5: 11.
    • (2012) BMC Biophysics , vol.5 , pp. 11
    • Kireeva, M.L.1    Opron, K.2    Seibold, S.A.3    Domecq, C.4    Cukier, R.I.5
  • 24
    • 78049347876 scopus 로고    scopus 로고
    • RNA Polymerase II with Open and Closed Trigger Loops: Active Site Dynamics and Nucleic Acid Translocation
    • Feig M, Burton ZF, (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
  • 25
    • 84863069608 scopus 로고    scopus 로고
    • Dynamics of Pyrophosphate Ion Release and Its Coupled Trigger Loop Motion from Closed to Open State in RNA Polymerase II
    • Da LT, Wang D, Huang X, (2012) Dynamics of Pyrophosphate Ion Release and Its Coupled Trigger Loop Motion from Closed to Open State in RNA Polymerase II. J Am Chem Soc 134: 2399-2406.
    • (2012) J Am Chem Soc , vol.134 , pp. 2399-2406
    • Da, L.T.1    Wang, D.2    Huang, X.3
  • 27
    • 82555205173 scopus 로고    scopus 로고
    • Fast transcription rates of RNA polymerase II in human cells
    • Maiuri P, Knezevich A, De Marco A, Mazza D, Kula A, et al. (2011) Fast transcription rates of RNA polymerase II in human cells. EMBO Rep 12: 1280-2185.
    • (2011) EMBO Rep , vol.12 , pp. 1280-2185
    • Maiuri, P.1    Knezevich, A.2    De Marco, A.3    Mazza, D.4    Kula, A.5
  • 29
    • 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, et al. (2003) Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase. EMBO J 22: 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
  • 31
    • 80051538984 scopus 로고    scopus 로고
    • RNA Transcript 3′-Proximal Sequence Affects Translocation Bias of RNA Polymerase
    • Hein PP, Palangat M, Landick R, (2011) RNA Transcript 3′-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
  • 32
    • 77449145343 scopus 로고    scopus 로고
    • RNA polymerase II flexibility during translocation from normal mode analysis
    • Feig M, Burton ZF, (2010) RNA polymerase II flexibility during translocation from normal mode analysis. Proteins: Structure, Function, and Bioinformatics 78: 434-446.
    • (2010) Proteins: Structure, Function, and Bioinformatics , vol.78 , pp. 434-446
    • Feig, M.1    Burton, Z.F.2
  • 33
    • 84867297989 scopus 로고    scopus 로고
    • Active site opening and closure control translocation of multisubunit RNA polymerase
    • Malinen AM, Turtola M, Parthiban M, Vainonen L, Johnson MS, et al. (2012) Active site opening and closure control translocation of multisubunit RNA polymerase. Nucleic Acids Res 40: 7442-7551.
    • (2012) Nucleic Acids Res , vol.40 , pp. 7442-7551
    • Malinen, A.M.1    Turtola, M.2    Parthiban, M.3    Vainonen, L.4    Johnson, M.S.5
  • 34
    • 10644237908 scopus 로고    scopus 로고
    • Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center
    • Batada NN, Westover KD, Bushnell DA, Levitt M, Kornberg RD, (2004) Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center. Proc Natl Acad Sci USA 101: 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
  • 35
    • 18944368782 scopus 로고    scopus 로고
    • Dynamic error correction and regulation of downstream bubble opening by human RNA polymerase II
    • Gong XQ, Zhang C, Feig M, Burton ZF, (2005) Dynamic error correction and regulation of downstream bubble opening by human RNA polymerase II. Mol Cell 18: 461-470.
    • (2005) Mol Cell , vol.18 , pp. 461-470
    • Gong, X.Q.1    Zhang, C.2    Feig, M.3    Burton, Z.F.4
  • 36
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • Yin YW, Steitz TA, (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
  • 38
    • 70349631761 scopus 로고    scopus 로고
    • Progress and challenges in the automated construction of Markov state models for full protein systems
    • Bowman GR, Beauchamp KA, Boxer G, Pande VS, (2009) Progress and challenges in the automated construction of Markov state models for full protein systems. J Chem Phys 131: 124101.
    • (2009) J Chem Phys , vol.131 , pp. 124101
    • Bowman, G.R.1    Beauchamp, K.A.2    Boxer, G.3    Pande, V.S.4
  • 39
    • 42149175435 scopus 로고    scopus 로고
    • Transition networks for modeling the kinetics of conformational change in macromolecules
    • Noé F, Fischer S, (2008) Transition networks for modeling the kinetics of conformational change in macromolecules. Curr Opin Struc Biol 18: 154-162.
    • (2008) Curr Opin Struc Biol , vol.18 , pp. 154-162
    • Noé, F.1    Fischer, S.2
  • 41
    • 34247338100 scopus 로고    scopus 로고
    • Automatic discovery of metastable states for the construction of Markov models of macromolecular conformational dynamics
    • Chodera JD, Singhal N, Pande VS, Dill KA, Swope WC, (2007) Automatic discovery of metastable states for the construction of Markov models of macromolecular conformational dynamics. J Chem Phys 126: 155101-155117.
    • (2007) J Chem Phys , vol.126 , pp. 155101-155117
    • Chodera, J.D.1    Singhal, N.2    Pande, V.S.3    Dill, K.A.4    Swope, W.C.5
  • 42
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, et al. (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 24: 1999-2012.
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5
  • 43
    • 0037495965 scopus 로고    scopus 로고
    • Development of polyphosphate parameters for use with the AMBER force field
    • Meagher KL, Redman LT, Carlson HA, (2003) Development of polyphosphate parameters for use with the AMBER force field. J Comput Chem 24: 1016-1025.
    • (2003) J Comput Chem , vol.24 , pp. 1016-1025
    • Meagher, K.L.1    Redman, L.T.2    Carlson, H.A.3
  • 47
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log (N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N log (N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 49
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi G, Donadio D, Parrinello M, (2007) Canonical sampling through velocity rescaling. J Chem Phys 126: 014101.
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 51
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • Isralewitz B, Gao M, Schulten K, (2001) Steered molecular dynamics and mechanical functions of proteins. Curr Opin Struc Biol 11: 224-230.
    • (2001) Curr Opin Struc Biol , vol.11 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 52
    • 63449118443 scopus 로고    scopus 로고
    • Using generalized ensemble simulations and Markov state models to identify conformational states
    • Bowman GR, Huang X, Pande VS, (2009) Using generalized ensemble simulations and Markov state models to identify conformational states. Methods 49: 197-201.
    • (2009) Methods , vol.49 , pp. 197-201
    • Bowman, G.R.1    Huang, X.2    Pande, V.S.3
  • 53
    • 79958212540 scopus 로고    scopus 로고
    • Simulating the T-Jump-Triggered Unfolding Dynamics of trpzip2 Peptide and Its Time-Resolved IR and Two-Dimensional IR Signals Using the Markov State Model Approach
    • Zhuang W, Cui RZ, Silva DA, Huang X, (2011) Simulating the T-Jump-Triggered Unfolding Dynamics of trpzip2 Peptide and Its Time-Resolved IR and Two-Dimensional IR Signals Using the Markov State Model Approach. J Phys Chem B 115: 5415-5424.
    • (2011) J Phys Chem B , vol.115 , pp. 5415-5424
    • Zhuang, W.1    Cui, R.Z.2    Silva, D.A.3    Huang, X.4
  • 54
    • 79958136745 scopus 로고    scopus 로고
    • A Role for Both Conformational Selection and Induced Fit in Ligand Binding by the LAO Protein
    • Silva DA, Bowman GR, Sosa-Peinado A, Huang X, (2011) A Role for Both Conformational Selection and Induced Fit in Ligand Binding by the LAO Protein. PLoS Comput Biol 7: e1002054.
    • (2011) PLoS Comput Biol , vol.7
    • Silva, D.A.1    Bowman, G.R.2    Sosa-Peinado, A.3    Huang, X.4
  • 56
    • 13544256263 scopus 로고    scopus 로고
    • Robust Perron cluster analysis in conformation dynamics
    • Deuflhard P, Weber M, (2005) Robust Perron cluster analysis in conformation dynamics. Linear Algebra Appl 398: 161-184.
    • (2005) Linear Algebra Appl , vol.398 , pp. 161-184
    • Deuflhard, P.1    Weber, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.