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Volumn 4, Issue C, 2002, Pages 139-151

Equilibrium and kinetic quantitative DNase I footprinting

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EID: 77957080402     PISSN: 1067568X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1067-568X(02)80008-1     Document Type: Article
Times cited : (2)

References (40)
  • 2
    • 0022437260 scopus 로고
    • Quantitative DNase footprint titration: A method for studying protein-DNA interactions
    • Brenowitz M., Senear D.F., Shea M.A., and Ackers G.K. Quantitative DNase footprint titration: A method for studying protein-DNA interactions. Meth. Enzymol. 130 (1986) 132-181
    • (1986) Meth. Enzymol. , vol.130 , pp. 132-181
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 3
    • 0022851259 scopus 로고
    • Energetics of cooperative protein-DNA interactions: Comparison between quantitative DNase footprint titration and filterbinding
    • Senear D.F., Brenowitz M., and Ackers G.K. Energetics of cooperative protein-DNA interactions: Comparison between quantitative DNase footprint titration and filterbinding. Biochemistry 25 (1986) 7344-7354
    • (1986) Biochemistry , vol.25 , pp. 7344-7354
    • Senear, D.F.1    Brenowitz, M.2    Ackers, G.K.3
  • 4
    • 0020510997 scopus 로고
    • Free energy coupling within macromolecules. The chemical work of ligand binding at the individual sites in co-operative systems
    • Ackers G.K., Shea M.A., and Smith F.R. Free energy coupling within macromolecules. The chemical work of ligand binding at the individual sites in co-operative systems. J. Mol. Biol. 170 (1983) 223-242
    • (1983) J. Mol. Biol. , vol.170 , pp. 223-242
    • Ackers, G.K.1    Shea, M.A.2    Smith, F.R.3
  • 6
    • 0001444289 scopus 로고
    • DNase I footprint analysis of protein-DNA binding
    • Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., and Struhl K. (Eds), John Wiley & Sons, New York
    • Brenowitz M., and Senear D.F. DNase I footprint analysis of protein-DNA binding. In: Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., and Struhl K. (Eds). Current Protocols in Molecular Biology (Unit 12.4) (1989), John Wiley & Sons, New York
    • (1989) Current Protocols in Molecular Biology (Unit 12.4)
    • Brenowitz, M.1    Senear, D.F.2
  • 9
    • 0029806242 scopus 로고    scopus 로고
    • Quantitative kinetics footprinting of protein-DNA association reactions
    • Hsieh M., and Brenowitz M. Quantitative kinetics footprinting of protein-DNA association reactions. Meth. Enzymol. 274 (1996) 478-492
    • (1996) Meth. Enzymol. , vol.274 , pp. 478-492
    • Hsieh, M.1    Brenowitz, M.2
  • 10
    • 0030845303 scopus 로고    scopus 로고
    • adi and the native dimeric gal repressor
    • adi and the native dimeric gal repressor. J. Biol. Chem. 272 (1997) 22092
    • (1997) J. Biol. Chem. , vol.272 , pp. 22092
    • Hsieh, M.1    Brenowitz, M.2
  • 11
    • 0031013756 scopus 로고    scopus 로고
    • Quantitative nucleic acids footprinting-thermodynamic and kinetic approaches
    • Petri V., and Brenowitz M. Quantitative nucleic acids footprinting-thermodynamic and kinetic approaches. Current Opinion in Biotechnology 8 (1997) 36-44
    • (1997) Current Opinion in Biotechnology , vol.8 , pp. 36-44
    • Petri, V.1    Brenowitz, M.2
  • 12
    • 0032500562 scopus 로고    scopus 로고
    • Cooperative non-specific DNA binding by octamerizing λ cI repressors: A site-specific thermodynamic analysis
    • Pray T.R., Bruz D.S., and Ackers G.K. Cooperative non-specific DNA binding by octamerizing λ cI repressors: A site-specific thermodynamic analysis. J. Mol. Biol. 282 (1998) 947-958
    • (1998) J. Mol. Biol. , vol.282 , pp. 947-958
    • Pray, T.R.1    Bruz, D.S.2    Ackers, G.K.3
  • 13
    • 0032478301 scopus 로고    scopus 로고
    • Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex
    • Streaker E.D., and Beckett D. Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex. Biochemistry 37 (1998) 3210-3219
    • (1998) Biochemistry , vol.37 , pp. 3210-3219
    • Streaker, E.D.1    Beckett, D.2
  • 14
    • 0032491380 scopus 로고    scopus 로고
    • 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
    • Craig M.L., Tsodikov O.V., McQuade K.L., Schlax Jr. P.E., Capp M.W., Saecker R.M., and Record Jr. T.M. 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. J. Mol. Biol. 283 (1998) 741-756
    • (1998) J. Mol. Biol. , vol.283 , pp. 741-756
    • Craig, M.L.1    Tsodikov, O.V.2    McQuade, K.L.3    Schlax Jr., P.E.4    Capp, M.W.5    Saecker, R.M.6    Record Jr., T.M.7
  • 15
    • 0029965491 scopus 로고    scopus 로고
    • Transcription revisited: A commentary on the 1995 Cold Spring Harbor Laboratory meeting, "Mechanisms of Eukaryotic Transcription"
    • McKnight S. Transcription revisited: A commentary on the 1995 Cold Spring Harbor Laboratory meeting, "Mechanisms of Eukaryotic Transcription". Genes and Development 10 (1996) 367-381
    • (1996) Genes and Development , vol.10 , pp. 367-381
    • McKnight, S.1
  • 16
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID (TFIID)
    • Burley S.K., and Roeder R.G. Biochemistry and structural biology of transcription factor IID (TFIID). Annul. Rev. Biochem. 65 (1996) 760-799
    • (1996) Annul. Rev. Biochem. , vol.65 , pp. 760-799
    • Burley, S.K.1    Roeder, R.G.2
  • 17
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y., Geiger J.H., Hahn S., and Sigler P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature 365 (1993) 512-520
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 18
    • 0027974851 scopus 로고
    • 1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAG
    • Kim J.L., and Burley S.K. 1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAG. Nature Struct. Biol. 1 (1994) 638-653
    • (1994) Nature Struct. Biol. , vol.1 , pp. 638-653
    • Kim, J.L.1    Burley, S.K.2
  • 21
    • 0033573008 scopus 로고    scopus 로고
    • TATA element recognition by the TATA box-binding protein has been conserved throughout evolution
    • Patikogluou G.A., Kim J.L., Sun L., Yang S.H., Kodadek T., and Burley S.K. TATA element recognition by the TATA box-binding protein has been conserved throughout evolution. Genes and Development 15 13 (1999) 3217-3230
    • (1999) Genes and Development , vol.15 , Issue.13 , pp. 3217-3230
    • Patikogluou, G.A.1    Kim, J.L.2    Sun, L.3    Yang, S.H.4    Kodadek, T.5    Burley, S.K.6
  • 22
    • 0022553616 scopus 로고
    • Role of Escherichia coli IHF protein in lambda site-specific recombination
    • Gardner J., and Nash H.A. Role of Escherichia coli IHF protein in lambda site-specific recombination. J. Mol. Biol. 191 (1986) 181-189
    • (1986) J. Mol. Biol. , vol.191 , pp. 181-189
    • Gardner, J.1    Nash, H.A.2
  • 23
    • 0027208111 scopus 로고
    • Function of IHF in λ DNA packaging. I. Identification of the strong binding site of integration host factor and the locus for intrinsic bending in cosB
    • Zin W., and Feiss M. Function of IHF in λ DNA packaging. I. Identification of the strong binding site of integration host factor and the locus for intrinsic bending in cosB. J. Mol. Biol. 230 (1993) 492-504
    • (1993) J. Mol. Biol. , vol.230 , pp. 492-504
    • Zin, W.1    Feiss, M.2
  • 24
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnA protein with protein HU or IHF
    • Hwang D.S., and Kornberg A. Opening of the replication origin of Escherichia coli by DnA protein with protein HU or IHF. J. Biol. Chem. 267 (1992) 23083-23086
    • (1992) J. Biol. Chem. , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 25
    • 0025282704 scopus 로고
    • Characterization of the integration host factor binding site in the ilvPG1 promoter region of the ilvGMEDA operon of Escherichia coli
    • Winkelman J.W., and Hatfield G.W. Characterization of the integration host factor binding site in the ilvPG1 promoter region of the ilvGMEDA operon of Escherichia coli. J. Biol. Chem. 265 (1990) 10055-10060
    • (1990) J. Biol. Chem. , vol.265 , pp. 10055-10060
    • Winkelman, J.W.1    Hatfield, G.W.2
  • 26
    • 0021044687 scopus 로고
    • The mechanism of phage 1 site-specific recombination: site-specific breakage of DNA by Int Topoisomerase
    • Craig N., and Nash H.A. The mechanism of phage 1 site-specific recombination: site-specific breakage of DNA by Int Topoisomerase. Cell 35 (1983) 795-803
    • (1983) Cell , vol.35 , pp. 795-803
    • Craig, N.1    Nash, H.A.2
  • 27
    • 0024340266 scopus 로고
    • The interaction of E. coli IHF protein with its specific binding sites
    • Yang S., and Nash H.A. The interaction of E. coli IHF protein with its specific binding sites. Cell 57 (1989) 869-880
    • (1989) Cell , vol.57 , pp. 869-880
    • Yang, S.1    Nash, H.A.2
  • 28
    • 0029561532 scopus 로고
    • Comparison of protein binding to DNA in vivo and in vitro: Defining an effective intracellular target
    • Yang S., and Nash H.A. Comparison of protein binding to DNA in vivo and in vitro: Defining an effective intracellular target. EMBO J. 14 (1995) 6292-6300
    • (1995) EMBO J. , vol.14 , pp. 6292-6300
    • Yang, S.1    Nash, H.A.2
  • 29
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn
    • Rice P.A., Yang S., Mizuuchi K., and Nash H.A. Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn. Cell 87 (1996) 1295-1306
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.2    Mizuuchi, K.3    Nash, H.A.4
  • 30
    • 0030450388 scopus 로고    scopus 로고
    • PCR-based development of DNA substrates containing modified bases: An efficient system for investigating the role of the exocyclic groupls in chemical and structural recognition by minor groove binding drugs and proteins
    • Bailly C., Payet D., Travers A.A., and Waring M.J. PCR-based development of DNA substrates containing modified bases: An efficient system for investigating the role of the exocyclic groupls in chemical and structural recognition by minor groove binding drugs and proteins. Proc. Natl. Acad. Sci. USA 93 (1996) 13623-13628
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13623-13628
    • Bailly, C.1    Payet, D.2    Travers, A.A.3    Waring, M.J.4
  • 31
    • 0029080688 scopus 로고
    • Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter
    • Petri V., Hsieh M., and Brenowitz M. Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter. Biochemistry 34 (1995) 9977-9984
    • (1995) Biochemistry , vol.34 , pp. 9977-9984
    • Petri, V.1    Hsieh, M.2    Brenowitz, M.3
  • 32
    • 0032506171 scopus 로고    scopus 로고
    • DNA Sequence-specific recognition by the "TATA" binding protein: Promoter dependent differences in the thermodynamics and kinetics
    • Petri V., Hsieh M., Jamison E., and Brenowitz M. DNA Sequence-specific recognition by the "TATA" binding protein: Promoter dependent differences in the thermodynamics and kinetics. Biochemistry 37 (1998) 15842-15849
    • (1998) Biochemistry , vol.37 , pp. 15842-15849
    • Petri, V.1    Hsieh, M.2    Jamison, E.3    Brenowitz, M.4
  • 33
    • 0026653485 scopus 로고
    • Simultaneous analysis for testing of models and parameter estimation
    • Senear D.F., and Bolen D.W. Simultaneous analysis for testing of models and parameter estimation. Meth. Enzymol. 210 (1992) 463-481
    • (1992) Meth. Enzymol. , vol.210 , pp. 463-481
    • Senear, D.F.1    Bolen, D.W.2
  • 34
    • 0026769027 scopus 로고
    • Analysis of site-specific interaction parameters in protein-DNA complexes
    • Koblan K.S., Bain D.L., Beckett D., Shea M.A., and Ackers G.K. Analysis of site-specific interaction parameters in protein-DNA complexes. Meth. Enzymol. 210 (1992) 405-425
    • (1992) Meth. Enzymol. , vol.210 , pp. 405-425
    • Koblan, K.S.1    Bain, D.L.2    Beckett, D.3    Shea, M.A.4    Ackers, G.K.5
  • 35
    • 0026664120 scopus 로고
    • Specific and nonspecific interactions of integration host factor with oligo DNAs and revealed by circular dichroism specitroscopy and filter binding assay
    • Kurumizaka H., Kanke F., Matsumoto U., and Shindo H. Specific and nonspecific interactions of integration host factor with oligo DNAs and revealed by circular dichroism specitroscopy and filter binding assay. Archives of Biochemistry and Biophysics 295 (1992) 297-301
    • (1992) Archives of Biochemistry and Biophysics , vol.295 , pp. 297-301
    • Kurumizaka, H.1    Kanke, F.2    Matsumoto, U.3    Shindo, H.4
  • 36
    • 77957071077 scopus 로고    scopus 로고
    • The integration host factor-DNA complex: Base-pair opening dynamics measured by NMR and kinetics of complex formation
    • Yale University
    • Dhavan G.M. The integration host factor-DNA complex: Base-pair opening dynamics measured by NMR and kinetics of complex formation. Ph. D. thesis (1999), Yale University
    • (1999) Ph. D. thesis
    • Dhavan, G.M.1
  • 37
    • 0026771275 scopus 로고
    • Sliding and intermolecular transfer of the lac repressor: Kinetic perturbation of a reaction intermediate by a distant DNA sequence
    • Ruusala T., and Crothers D.M. Sliding and intermolecular transfer of the lac repressor: Kinetic perturbation of a reaction intermediate by a distant DNA sequence. Proc. Natl. Acad. Sci. USA 89 (1992) 4903-4907
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4903-4907
    • Ruusala, T.1    Crothers, D.M.2
  • 38
    • 0033603388 scopus 로고    scopus 로고
    • Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex
    • Parkhurst K.M., Richards R.M., Brenowitz M., and Parkhurst L.J. Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex. J. Mol. Biol. 289 (1999) 1327-1341
    • (1999) J. Mol. Biol. , vol.289 , pp. 1327-1341
    • Parkhurst, K.M.1    Richards, R.M.2    Brenowitz, M.3    Parkhurst, L.J.4
  • 39
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates
    • Johnson K.A. Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates. Meth. Enzymol. 249 (1995) 38-61
    • (1995) Meth. Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 40
    • 0019867850 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: Kinetic measurements and conclusions
    • Winter R.B., Berg O.G., and von Hippel P.H. Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: Kinetic measurements and conclusions. Biochemistry 20 (1981) 6961-6977
    • (1981) Biochemistry , vol.20 , pp. 6961-6977
    • Winter, R.B.1    Berg, O.G.2    von Hippel, P.H.3


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