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Volumn 95, Issue 5, 2008, Pages 2423-2433

T7 RNA polymerase studied by force measurements varying cofactor concentration

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE T7 RNA POLYMERASE; DNA DIRECTED RNA POLYMERASE; MAGNESIUM; NUCLEOTIDE; VIRUS PROTEIN;

EID: 51649113736     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.125096     Document Type: Article
Times cited : (50)

References (38)
  • 1
    • 0026728955 scopus 로고
    • The single-nucleotide addition cycle in transcription: A biophysical and biochemical perspective
    • Erie, D. A., T. D. Yager, and P. H. Vonhippel. 1992. The single-nucleotide addition cycle in transcription: a biophysical and biochemical perspective. Annu. Rev. Biophys. Biomol. Struct. 21:379-415.
    • (1992) Annu. Rev. Biophys. Biomol. Struct , vol.21 , pp. 379-415
    • Erie, D.A.1    Yager, T.D.2    Vonhippel, P.H.3
  • 3
    • 0034737593 scopus 로고    scopus 로고
    • Single-molecule study of transcriptional pausing and arrest by E-coli RNA polymerase
    • Davenport, R. J., G. J. L. Wuite, R. Landick, and C. Bustamante. 2000. Single-molecule study of transcriptional pausing and arrest by E-coli RNA polymerase. Science. 287:2497-2500.
    • (2000) Science , vol.287 , pp. 2497-2500
    • Davenport, R.J.1    Wuite, G.J.L.2    Landick, R.3    Bustamante, C.4
  • 4
    • 0034594940 scopus 로고    scopus 로고
    • Single-molecule studies of the effect of template tension on T7 DNA polymerase activity
    • Wuite, G. J. L., S. B. Smith, M. Young, D. Keller, and C. Bustamante. 2000. Single-molecule studies of the effect of template tension on T7 DNA polymerase activity. Nature. 404:103-106.
    • (2000) Nature , vol.404 , pp. 103-106
    • Wuite, G.J.L.1    Smith, S.B.2    Young, M.3    Keller, D.4    Bustamante, C.5
  • 5
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage φ29 portal motor can package DNA against a large internal force
    • Smith, D. E., S. J. Tans, S. B. Smith, S. Grimes, D. L. Anderson, and C. Bustamante. 2001. The bacteriophage φ29 portal motor can package DNA against a large internal force. Nature. 413:748-752.
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 6
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher, K., M. J. Schnitzer, and S. M. Block. 1999. Single kinesin molecules studied with a molecular force clamp. Nature. 400:184-189.
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 8
    • 0032582494 scopus 로고    scopus 로고
    • Force and velocity measured for single molecules of RNA polymerase
    • Wang, M. D., M. J. Schnitzer, H. Yin, R. Landick, J. Gelles, and S. M. Block. 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
  • 10
    • 0034710990 scopus 로고    scopus 로고
    • Replication by a single DNA polymerase of a stretched single-stranded DNA
    • Maier, B., D. Bensimon, and V. Croquette. 2000. Replication by a single DNA polymerase of a stretched single-stranded DNA. Proc. Natl. Acad. Sci. USA. 97:12002-12007.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12002-12007
    • Maier, B.1    Bensimon, D.2    Croquette, V.3
  • 11
    • 0345047725 scopus 로고    scopus 로고
    • Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking
    • Neuman, K. C., E. A. Abbondanzieri, R. Landick, J. Gelles, and S. M. Block. 2003. Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking. Cell. 115:437-447.
    • (2003) Cell , vol.115 , pp. 437-447
    • Neuman, K.C.1    Abbondanzieri, E.A.2    Landick, R.3    Gelles, J.4    Block, S.M.5
  • 14
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • Yin, Y. W., and T. A. Steitz. 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
  • 16
    • 0942298127 scopus 로고    scopus 로고
    • Promoter binding, initiation, and elongation by bacteriophage T7 RNA polymerase: A single-molecule view of the transcription cycle
    • Skinner, G. M., C. G. Baumann, D. M. Quinn, J. E. Molloy, and J. G. Hoggett. 2004. Promoter binding, initiation, and elongation by bacteriophage T7 RNA polymerase: a single-molecule view of the transcription cycle. J. Biol. Chem. 279:3239-3244.
    • (2004) J. Biol. Chem , vol.279 , pp. 3239-3244
    • Skinner, G.M.1    Baumann, C.G.2    Quinn, D.M.3    Molloy, J.E.4    Hoggett, J.G.5
  • 18
    • 85056017495 scopus 로고    scopus 로고
    • Unravelling the mechanism of RNA-polymerase forward motion by using mechanical force
    • Thomen, P., P. J. Lopez, and F. Heslot. 2005. Unravelling the mechanism of RNA-polymerase forward motion by using mechanical force. Phys. Rev. Lett. 94:128102.
    • (2005) Phys. Rev. Lett , vol.94 , pp. 128102
    • Thomen, P.1    Lopez, P.J.2    Heslot, F.3
  • 19
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin, Y. W., and A. A. Steitz. 2002. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science. 298:1387-1395.
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, A.A.2
  • 21
    • 0036198476 scopus 로고    scopus 로고
    • Unzipping DNA with optical tweezers: High sequence sensitivity and force flips
    • Bockelmann, U., P. Thomen, B. Essevaz-Roulet, V. Viasnoff, and F. Heslot. 2002. Unzipping DNA with optical tweezers: high sequence sensitivity and force flips. Biophys. J. 82:1537-1553.
    • (2002) Biophys. J , vol.82 , pp. 1537-1553
    • Bockelmann, U.1    Thomen, P.2    Essevaz-Roulet, B.3    Viasnoff, V.4    Heslot, F.5
  • 22
    • 0028224704 scopus 로고
    • Effects of solution conditions on the steady-state kinetics of initiation of transcription by T7 RNA polymerase
    • Maslak, M., and C. T. Martin. 1994. Effects of solution conditions on the steady-state kinetics of initiation of transcription by T7 RNA polymerase. Biochemistry. 33:6918-6924.
    • (1994) Biochemistry , vol.33 , pp. 6918-6924
    • Maslak, M.1    Martin, C.T.2
  • 23
    • 0035971214 scopus 로고    scopus 로고
    • Scanning mutagenesis reveals roles for helix N of the bacteriophage T7 RNA polymerase thumb subdomain in transcription complex stability, pausing, and termination
    • Brieba, L. G., V. Gopal, and R. Sousa. 2001. Scanning mutagenesis reveals roles for helix N of the bacteriophage T7 RNA polymerase thumb subdomain in transcription complex stability, pausing, and termination. J. Biol. Chem. 276:10306-10313.
    • (2001) J. Biol. Chem , vol.276 , pp. 10306-10313
    • Brieba, L.G.1    Gopal, V.2    Sousa, R.3
  • 24
    • 33751156715 scopus 로고
    • Stiff chains and filaments under tension
    • Odijk, T. 1995. Stiff chains and filaments under tension. Macromolecules. 28:7016-7018.
    • (1995) Macromolecules , vol.28 , pp. 7016-7018
    • Odijk, T.1
  • 25
    • 19244382579 scopus 로고    scopus 로고
    • Diversity in the rates of transcript elongation by single RNA polymerase molecules
    • Tolic-Norrelykke, S. F., A. M. Engh, R. Landick, and J. Gelles. 2004. Diversity in the rates of transcript elongation by single RNA polymerase molecules. J. Biol. Chem. 279:3292-3299.
    • (2004) J. Biol. Chem , vol.279 , pp. 3292-3299
    • Tolic-Norrelykke, S.F.1    Engh, A.M.2    Landick, R.3    Gelles, J.4
  • 27
    • 0036681040 scopus 로고    scopus 로고
    • Energetics of Brownian motors: A review
    • Parrondo, J. M. R., and B. J. De Cisneros. 2002. Energetics of Brownian motors: a review. Appl. Phys. A. 75:179-191.
    • (2002) Appl. Phys. A , vol.75 , pp. 179-191
    • Parrondo, J.M.R.1    De Cisneros, B.J.2
  • 28
    • 0031003997 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of a Brownian motor
    • Astumian, R. D. 1997. Thermodynamics and kinetics of a Brownian motor. Science. 276:917-922.
    • (1997) Science , vol.276 , pp. 917-922
    • Astumian, R.D.1
  • 29
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li, Y., S. Korolev, and G. Waksman. 1998. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17:7514-7525.
    • (1998) EMBO J , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 30
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Åresolution
    • Doublie, S., S. Tabor, A. M. Long, C. C. Richardson, and T. Ellenberger. 1998. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Åresolution. Nature. 391:251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 31
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: Implications for drug resistance
    • Huang, H. F., R. Chopra, G. L. Verdine, and S. C. Harrison. 1998. Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: implications for drug resistance. Science. 282:1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.F.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 32
    • 33645097171 scopus 로고    scopus 로고
    • Translocation by T7 RNA polymerase: A sensitively Brownian ratchet
    • Guo, Q., and R. Sousa. 2006. Translocation by T7 RNA polymerase: a sensitively Brownian ratchet. J. Mol. Biol. 358:241-254.
    • (2006) J. Mol. Biol , vol.358 , pp. 241-254
    • Guo, Q.1    Sousa, R.2
  • 33
    • 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., E. P. Tchesnokov, and M. Gotte. 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
  • 34
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam, C. A., and T. A. Steitz. 1998. Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8:54-63.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 35
    • 0017146584 scopus 로고
    • 2- and other ions in solution: Calculation of true concentrations of species present in mixtures of associating ions
    • 2- and other ions in solution: calculation of true concentrations of species present in mixtures of associating ions. Biochem. J. 159:1-5.
    • (1976) Biochem. J , vol.159 , pp. 1-5
    • Storer, A.C.1    Cornishbowden, A.2
  • 37
    • 1842301055 scopus 로고    scopus 로고
    • Modeling and optimization of a batch process for in vitro RNA production
    • Young, J. S., W. F. Ramirez, and R. H. Davis. 1997. Modeling and optimization of a batch process for in vitro RNA production. Biotechnol. Bioeng. 56:210-220.
    • (1997) Biotechnol. Bioeng , vol.56 , pp. 210-220
    • Young, J.S.1    Ramirez, W.F.2    Davis, R.H.3
  • 38
    • 0030026560 scopus 로고    scopus 로고
    • Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription
    • Woody, A. Y. M., S. S. Eaton, P. A. Osumi-Davis, and R. W. Woody. 1996. Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription. Biochemistry. 35:144-152.
    • (1996) Biochemistry , vol.35 , pp. 144-152
    • Woody, A.Y.M.1    Eaton, S.S.2    Osumi-Davis, P.A.3    Woody, R.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.