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Volumn 283, Issue 4, 1998, Pages 741-756

DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex: Evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA

Author keywords

Footprinting; Open complex formation; RNA polymerase; Transcription initiation; P(R) promoter

Indexed keywords

DEOXYRIBONUCLEASE I; HEPARIN; RNA POLYMERASE;

EID: 0032491380     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2129     Document Type: Article
Times cited : (103)

References (46)
  • 1
    • 0031551578 scopus 로고    scopus 로고
    • Two conformations of RNA polymerase II revealed by electron crystallography
    • Asturias J.F., Meredith G.D., Poglitsch C.L., Kornberg R.D. Two conformations of RNA polymerase II revealed by electron crystallography. J. Mol. Biol. 272:1997;536-540
    • (1997) J. Mol. Biol. , vol.272 , pp. 536-540
    • Asturias, J.F.1    Meredith, G.D.2    Poglitsch, C.L.3    Kornberg, R.D.4
  • 2
    • 0028815976 scopus 로고
    • The transcriptional activator protein FIS: DNA interactions and cooperative interactions with RNA polymerase at the Escherichia coli rrnB P1 promoter
    • Bokal A.J.I.V., Ross W., Gourse R.L. The transcriptional activator protein FIS DNA interactions and cooperative interactions with RNA polymerase at the Escherichia coli rrnB P1 promoter. J. Mol. Biol. 245:1995;197-207
    • (1995) J. Mol. Biol. , vol.245 , pp. 197-207
    • Bokal, A.J.I.V.1    Ross, W.2    Gourse, R.L.3
  • 3
    • 0022437260 scopus 로고
    • Quantitative DNase footprint titration: A method for studying protein-DNA interactions
    • Brenowitz M., Senear D.F., Shea M.A., Ackers G.K. Quantitative DNase footprint titration a method for studying protein-DNA interactions. Methods Enzymol. 130:1986;132-181
    • (1986) Methods Enzymol. , vol.130 , pp. 132-181
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 4
    • 0021857751 scopus 로고
    • Kinetics of open complex formation between Escherichia coli RNA polymerase and the lac UV5 promoter. Evidence for a sequential mechanism involving three steps
    • Buc H., McClure W.R. Kinetics of open complex formation between Escherichia coli RNA polymerase and the lac UV5 promoter. Evidence for a sequential mechanism involving three steps. Biochemistry. 24:1985;2712-2723
    • (1985) Biochemistry , vol.24 , pp. 2712-2723
    • Buc, H.1    McClure, W.R.2
  • 5
    • 0016748261 scopus 로고
    • A procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatography
    • Burgess R.R., Jendrisak J.J. A procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatography. Biochemistry. 14:1975;4634-4638
    • (1975) Biochemistry , vol.14 , pp. 4634-4638
    • Burgess, R.R.1    Jendrisak, J.J.2
  • 7
    • 85030346405 scopus 로고    scopus 로고
    • Madison, WI: University of Wisconsin-Madison. PhD thesis
    • R promoter. 1996;University of Wisconsin-Madison, Madison, WI. PhD thesis
    • (1996) R Promoter
    • Craig, M.L.1
  • 8
    • 0028789430 scopus 로고
    • 2+ binding and its structural consequences at the transcription start site
    • 2+ binding and its structural consequences at the transcription start site. Biochemistry. 34:1995;15624-15632
    • (1995) Biochemistry , vol.34 , pp. 15624-15632
    • Craig, M.L.1    Suh, W.C.2    Record Jr., M.T.3
  • 9
    • 0024342908 scopus 로고
    • Three-dimensional structure of Escherichia coli RNA polymerase holoenzyme determined by electron crystallography
    • Darst S.A., Kubalek E.W., Kornberg R.D. Three-dimensional structure of Escherichia coli RNA polymerase holoenzyme determined by electron crystallography. Nature. 340:1989;730-732
    • (1989) Nature , vol.340 , pp. 730-732
    • Darst, S.A.1    Kubalek, E.W.2    Kornberg, R.D.3
  • 10
    • 0029094575 scopus 로고
    • Open complex formation by Escherichia coli RNA polymerase: The mechanism of polymerase-induced strand separation of double helical DNA
    • deHaseth P.L., Helmann J.D. Open complex formation by Escherichia coli RNA polymerase the mechanism of polymerase-induced strand separation of double helical DNA. Mol. Microbiol. 16:1995;817-824
    • (1995) Mol. Microbiol. , vol.16 , pp. 817-824
    • Dehaseth, P.L.1    Helmann, J.D.2
  • 11
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublié S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 13
    • 0017684749 scopus 로고
    • A simple procedure for resolution of Escherichia coli RNA polymerase holoenzyme from core polymerase
    • Gonzalez N., Wiggs J., Chamberlin M.J. A simple procedure for resolution of Escherichia coli RNA polymerase holoenzyme from core polymerase. Arch. Biochem. Biophys. 182:1977;404-408
    • (1977) Arch. Biochem. Biophys. , vol.182 , pp. 404-408
    • Gonzalez, N.1    Wiggs, J.2    Chamberlin, M.J.3
  • 14
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J.-H., Spolar R.S., Record M.T. Jr. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209:1989;801-816
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record Jr., M.T.3
  • 15
    • 0022432952 scopus 로고
    • The pathway of E. coli RNA polymerase-promoter complex formation as visualized by footprinting
    • Hofer B., Muller D., Koster H. The pathway of E. coli RNA polymerase-promoter complex formation as visualized by footprinting. Nucl. Acids Res. 16:1985;5995-6013
    • (1985) Nucl. Acids Res. , vol.16 , pp. 5995-6013
    • Hofer, B.1    Muller, D.2    Koster, H.3
  • 16
  • 17
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391:1998;304-307
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 18
    • 0023645694 scopus 로고
    • The 0°C closed complexes between Escherichia coli RNA polymerase and two promoters, T7-A3 and lacUV5
    • Kovacic R.T. The 0°C closed complexes between Escherichia coli RNA polymerase and two promoters, T7-A3 and lacUV5. J. Biol. Chem. 262:1987;13654-13661
    • (1987) J. Biol. Chem. , vol.262 , pp. 13654-13661
    • Kovacic, R.T.1
  • 19
    • 0026354983 scopus 로고
    • DNase I-induced DNA conformation: 2 Å structure of a DNase I-octamer complex
    • Lahm A., Suck D. DNase I-induced DNA conformation 2 Å structure of a DNase I-octamer complex. J. Mol. Biol. 262:1991;645-667
    • (1991) J. Mol. Biol. , vol.262 , pp. 645-667
    • Lahm, A.1    Suck, D.2
  • 20
    • 0026808773 scopus 로고
    • Transcription activation by cAMP receptor protein (CRP) at the Escherichia coli gal P1 promoter. Crucial role for the spacing between the CRP binding site and the -10 region
    • Lavigne M., Kolb A., Buc H. Transcription activation by cAMP receptor protein (CRP) at the Escherichia coli gal P1 promoter. Crucial role for the spacing between the CRP binding site and the -10 region. Biochemistry. 31:1992;9647-9656
    • (1992) Biochemistry , vol.31 , pp. 9647-9656
    • Lavigne, M.1    Kolb, A.2    Buc, H.3
  • 22
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • Maxam A.M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:1980;499-560
    • (1980) Methods Enzymol , vol.65 , pp. 499-560
    • Maxam, A.M.1    Gilbert, W.2
  • 24
    • 0025785249 scopus 로고
    • Development of RNA polymerase-promoter contacts during open complex formation
    • Mecsas J., Cowing D.W., Gross C.A. Development of RNA polymerase-promoter contacts during open complex formation. J. Mol. Biol. 220:1991;585-597
    • (1991) J. Mol. Biol. , vol.220 , pp. 585-597
    • Mecsas, J.1    Cowing, D.W.2    Gross, C.A.3
  • 25
    • 0028877383 scopus 로고
    • Role of curved DNA in binding to Escherichia coli RNA polymerase to promoters
    • Nickerson C.A., Achberger E.C. Role of curved DNA in binding to Escherichia coli RNA polymerase to promoters. J. Bacteriol. 177:1995;5756-5761
    • (1995) J. Bacteriol , vol.177 , pp. 5756-5761
    • Nickerson, C.A.1    Achberger, E.C.2
  • 26
    • 0029818631 scopus 로고    scopus 로고
    • Transcription processivity: Protein-DNA interactions holding together the elongation complex
    • Nudler E., Avetissova E., Markovtsov V., Goldfarb A. Transcription processivity protein-DNA interactions holding together the elongation complex. Science. 273:1996;211-217
    • (1996) Science , vol.273 , pp. 211-217
    • Nudler, E.1    Avetissova, E.2    Markovtsov, V.3    Goldfarb, A.4
  • 27
    • 0028566215 scopus 로고
    • Polymerase structures and mechanism
    • Pelletier H. Polymerase structures and mechanism. Science. 266:1994;2025-2026
    • (1994) Science , vol.266 , pp. 2025-2026
    • Pelletier, H.1
  • 28
    • 0028875725 scopus 로고
    • Three-dimensional structure of E. coli core RNA polymerase: Promoter binding and elongation conformations of the enzyme
    • Polyakov A., Severinova E., Darst S.A. Three-dimensional structure of E. coli core RNA polymerase promoter binding and elongation conformations of the enzyme. Cell. 83:1995;365-373
    • (1995) Cell , vol.83 , pp. 365-373
    • Polyakov, A.1    Severinova, E.2    Darst, S.A.3
  • 32
    • 0021840415 scopus 로고
    • R promoter interaction: Assignment of the kinetic steps corresponding to protein conformational change and DNA opening
    • R promoter interaction assignment of the kinetic steps corresponding to protein conformational change and DNA opening. J. Mol. Biol. 184:1985;441-453
    • (1985) J. Mol. Biol. , vol.184 , pp. 441-453
    • Roe, J.-H.1    Burgess, R.R.2    Record Jr., M.T.3
  • 33
  • 34
    • 0025369026 scopus 로고
    • Topography of intermediates in transcription initiation of E. coli
    • Schickor P., Metzger W., Werel W., Lederer H., Heumann H. Topography of intermediates in transcription initiation of E. coli. EMBO J. 9:1990;2215-2220
    • (1990) EMBO J. , vol.9 , pp. 2215-2220
    • Schickor, P.1    Metzger, W.2    Werel, W.3    Lederer, H.4    Heumann, H.5
  • 35
    • 0344473474 scopus 로고
    • Madison, WI: University of Wilconsin-Madison. PhD thesis
    • R promoter. 1995;University of Wilconsin-Madison, Madison, WI. PhD thesis
    • (1995) R Promoter
    • Schlax, P.E.1
  • 36
    • 1542642108 scopus 로고
    • Rapid estimation of DNA concentration by ethidium bromide dot quantitation
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, Struhl K. NY: John Wiley & Sons, Inc
    • Selden R.F., Chory J. Rapid estimation of DNA concentration by ethidium bromide dot quantitation. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. vol. 2.6.7:1987;John Wiley & Sons, Inc, NY
    • (1987) Current Protocols in Molecular Biology , vol.267
    • Selden, R.F.1    Chory, J.2
  • 37
    • 0031456021 scopus 로고    scopus 로고
    • A mutant RNA polymerase that forms unusual open promoter complexes
    • Severinov K., Darst S.A. A mutant RNA polymerase that forms unusual open promoter complexes. Proc. Natl Acad. Sci. USA. 94:1997;13481-13486
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13481-13486
    • Severinov, K.1    Darst, S.A.2
  • 38
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution
    • Sousa R., Chung Y.J., Rose J.P., Wang B.C. Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature. 364:1993;593-599
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1    Chung, Y.J.2    Rose, J.P.3    Wang, B.C.4
  • 39
    • 0028035156 scopus 로고
    • The thumb's knuckle. Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNAP polymerase
    • Sousa R., Rose J.P., Wang B.C. The thumb's knuckle. Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNAP polymerase. J. Mol. Biol. 244:1994;6-12
    • (1994) J. Mol. Biol. , vol.244 , pp. 6-12
    • Sousa, R.1    Rose, J.P.2    Wang, B.C.3
  • 40
    • 0021827364 scopus 로고
    • Changes in the DNA structure of the lac UV5 promoter during formation of an open complex with Escherichia coli RNA polymerase
    • Spassky L.A., Kirkegaard K., Buc H. Changes in the DNA structure of the lac UV5 promoter during formation of an open complex with Escherichia coli RNA polymerase. Biochemistry. 24:1985;2723-2730
    • (1985) Biochemistry , vol.24 , pp. 2723-2730
    • Spassky, L.A.1    Kirkegaard, K.2    Buc, H.3
  • 41
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., Record M.T. Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:1994;777-784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 42
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz T.A., Smerdom S.J., Jåger J., Joyce C.M. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science. 266:1994;2022-2025
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1    Smerdom, S.J.2    Jåger, J.3    Joyce, C.M.4


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