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Volumn 51, Issue 19, 2012, Pages 4028-4034

Allosteric control of cAMP receptor binding dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC CONTROL; CYCLIC AMP RECEPTOR PROTEINS; DIFFUSION CONTROL; INTRINSIC FLUORESCENCE; LOW SALT CONCENTRATION; PHOTOREACTIONS; PHYSIOLOGICAL CONCENTRATIONS; PHYSIOLOGICAL SALT CONCENTRATIONS; REACTION STEPS; RECEPTOR BINDING; SENSITIVE INDICATOR; TIME RANGE;

EID: 84861125096     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3002874     Document Type: Article
Times cited : (2)

References (35)
  • 1
    • 0014779269 scopus 로고
    • Mechanism of Activation of Catabolite-Sensitive Genes: A Positive Control System
    • Zubay, G., Schwartz, D., and Beckwith, J. (1970) Mechanism of Activation of Catabolite-Sensitive Genes: A Positive Control System Proc. Natl. Acad. Sci. U.S.A. 66, 104-110
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.66 , pp. 104-110
    • Zubay, G.1    Schwartz, D.2    Beckwith, J.3
  • 2
    • 7444245668 scopus 로고    scopus 로고
    • Identification of the CRP regulon using in vitro and in vivo transcriptional profiling
    • Zheng, D. L., Constantinidou, C., Hobman, J. L., and Minchin, S. D. (2004) Identification of the CRP regulon using in vitro and in vivo transcriptional profiling Nucleic Acids Res. 32, 5874-5893
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5874-5893
    • Zheng, D.L.1    Constantinidou, C.2    Hobman, J.L.3    Minchin, S.D.4
  • 3
    • 0021245317 scopus 로고
    • Cyclic AMP Receptor Protein: Role in Transcription Activation
    • de Crombrugghe, B., Busby, S., and Buc, H. (1984) Cyclic AMP Receptor Protein: Role in Transcription Activation Science 224, 831-838
    • (1984) Science , vol.224 , pp. 831-838
    • De Crombrugghe, B.1    Busby, S.2    Buc, H.3
  • 4
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
    • McKay, D. B. and Steitz, T. A. (1981) Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA Nature 290, 744-749
    • (1981) Nature , vol.290 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 5
    • 0025914242 scopus 로고
    • Crystal Structure of a CAP-DNA Complex: The DNA Is Bent by 90°
    • Schultz, S. C., Shields, G. C., and Steitz, T. A. (1991) Crystal Structure of a CAP-DNA Complex: The DNA Is Bent by 90° Science 253, 1001-1007
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 6
    • 0000445736 scopus 로고    scopus 로고
    • The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer
    • Passner, J. M. and Steitz, T. A. (1997) The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer Proc. Natl. Acad. Sci. U.S.A. 94, 2843-2847
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 7
    • 0030593510 scopus 로고    scopus 로고
    • Structure of the CAP-DNA complex at 2.5 angstrom resolution: A complete picture of the protein-DNA interface
    • Parkinson, G., Wilson, C., Gunasekera, A., Ebright, Y. W., Ebright, R. E., and Berman, H. M. (1996) Structure of the CAP-DNA complex at 2.5 angstrom resolution: A complete picture of the protein-DNA interface J. Mol. Biol. 260, 395-408
    • (1996) J. Mol. Biol. , vol.260 , pp. 395-408
    • Parkinson, G.1    Wilson, C.2    Gunasekera, A.3    Ebright, Y.W.4    Ebright, R.E.5    Berman, H.M.6
  • 9
    • 70349734666 scopus 로고    scopus 로고
    • Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
    • Sharma, H., Yu, S. N., Kong, J. L., Wang, J. M., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding Proc. Natl. Acad. Sci. U.S.A. 106, 16604-16609
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16604-16609
    • Sharma, H.1    Yu, S.N.2    Kong, J.L.3    Wang, J.M.4    Steitz, T.A.5
  • 10
    • 0035929295 scopus 로고    scopus 로고
    • Mean DNA bend angle and distribution of DNA bend angles in the CAP-DNA complex in solution
    • Kapanidis, A. N., Ebright, Y. W., Ludescher, R. D., Chan, S., and Ebright, R. H. (2001) Mean DNA bend angle and distribution of DNA bend angles in the CAP-DNA complex in solution J. Mol. Biol. 312, 453-468
    • (2001) J. Mol. Biol. , vol.312 , pp. 453-468
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ludescher, R.D.3    Chan, S.4    Ebright, R.H.5
  • 11
    • 0037995648 scopus 로고    scopus 로고
    • Determinants of DNA bending in the DNA-cyclic AMP receptor protein complexes in Escherichia coli
    • Lin, S. H. and Lee, J. C. (2003) Determinants of DNA bending in the DNA-cyclic AMP receptor protein complexes in Escherichia coli Biochemistry 42, 4809-4818
    • (2003) Biochemistry , vol.42 , pp. 4809-4818
    • Lin, S.H.1    Lee, J.C.2
  • 12
    • 0026680634 scopus 로고
    • Solution studies on the structure of bent DNA in the cAMP receptor protein-lac DNA complex
    • Heyduk, T. and Lee, J. C. (1992) Solution studies on the structure of bent DNA in the cAMP receptor protein-lac DNA complex Biochemistry 31, 5165-5171
    • (1992) Biochemistry , vol.31 , pp. 5165-5171
    • Heyduk, T.1    Lee, J.C.2
  • 13
    • 0032512613 scopus 로고    scopus 로고
    • Measurement of the DNA bend angle induced by the catabolite activator protein using Monte Carlo simulation of cyclization kinetics
    • Kahn, J. D. and Crothers, D. M. (1998) Measurement of the DNA bend angle induced by the catabolite activator protein using Monte Carlo simulation of cyclization kinetics J. Mol. Biol. 276, 287-309
    • (1998) J. Mol. Biol. , vol.276 , pp. 287-309
    • Kahn, J.D.1    Crothers, D.M.2
  • 14
    • 77954178921 scopus 로고    scopus 로고
    • Allosteric Control of Promoter DNA Bending by Cyclic AMP Receptor and Cyclic AMP
    • Porschke, D. (2010) Allosteric Control of Promoter DNA Bending by Cyclic AMP Receptor and Cyclic AMP Biochemistry 49, 5553-5559
    • (2010) Biochemistry , vol.49 , pp. 5553-5559
    • Porschke, D.1
  • 15
    • 0021342434 scopus 로고
    • Kinetics and Mechanism in the Reaction of Gene Regulatory Proteins with DNA
    • Fried, M. G. and Crothers, D. M. (1984) Kinetics and Mechanism in the Reaction of Gene Regulatory Proteins with DNA J. Mol. Biol. 172, 263-282
    • (1984) J. Mol. Biol. , vol.172 , pp. 263-282
    • Fried, M.G.1    Crothers, D.M.2
  • 16
    • 14644390330 scopus 로고    scopus 로고
    • Fluorescence quenching and kinetic studies of conformational changes induced by DNA and cAMP binding to cAMP receptor protein from Escherichia coli
    • Tworzydlo, M., Polit, A., Mikolajczak, J., and Wasylewski, Z. (2005) Fluorescence quenching and kinetic studies of conformational changes induced by DNA and cAMP binding to cAMP receptor protein from Escherichia coli FEBS J. 272, 1103-1116
    • (2005) FEBS J. , vol.272 , pp. 1103-1116
    • Tworzydlo, M.1    Polit, A.2    Mikolajczak, J.3    Wasylewski, Z.4
  • 17
    • 84860273712 scopus 로고    scopus 로고
    • Structures during binding of cAMP receptor to promoter DNA: Promoter search slowed by non-specific sites
    • Porschke, D. (2012) Structures during binding of cAMP receptor to promoter DNA: Promoter search slowed by non-specific sites Eur. Biophys. J. 41, 415-424
    • (2012) Eur. Biophys. J. , vol.41 , pp. 415-424
    • Porschke, D.1
  • 18
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase Anal. Biochem. 237, 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 19
    • 71549142265 scopus 로고    scopus 로고
    • DynaFit: A Software Package for Enzymology
    • Kuzmic, P. (2009) DynaFit: A Software Package for Enzymology Methods Enzymol. 467, 247-280
    • (2009) Methods Enzymol. , vol.467 , pp. 247-280
    • Kuzmic, P.1
  • 20
    • 0023785204 scopus 로고
    • Scanning Calorimetric Study of the Thermal Unfolding of Catabolite Activator Protein from Escherichia coli in the Absence and Presence of Cyclic Mononucleotides
    • Ghosaini, L. R., Brown, A. M., and Sturtevant, J. M. (1988) Scanning Calorimetric Study of the Thermal Unfolding of Catabolite Activator Protein from Escherichia coli in the Absence and Presence of Cyclic Mononucleotides Biochemistry 27, 5257-5261
    • (1988) Biochemistry , vol.27 , pp. 5257-5261
    • Ghosaini, L.R.1    Brown, A.M.2    Sturtevant, J.M.3
  • 21
    • 0019138202 scopus 로고
    • An Equilibrium Study of the Cooperative Binding of Adenosine Cyclic 3′,5′-Monophosphate and Guanosine Cyclic 3′,5′- Monophosphate to the Adenosine Cyclic 3′,5′-Monophosphate Receptor Protein from Escherichia coli
    • Takahashi, M., Blazy, B., and Baudras, A. (1980) An Equilibrium Study of the Cooperative Binding of Adenosine Cyclic 3′,5′-Monophosphate and Guanosine Cyclic 3′,5′-Monophosphate to the Adenosine Cyclic 3′,5′-Monophosphate Receptor Protein from Escherichia coli Biochemistry 19, 5124-5130
    • (1980) Biochemistry , vol.19 , pp. 5124-5130
    • Takahashi, M.1    Blazy, B.2    Baudras, A.3
  • 22
    • 0037126706 scopus 로고    scopus 로고
    • Linkage of multiequilibria in DNA recognition by the D53H Escherichia coli, cAMP receptor protein
    • Lin, S. H. and Lee, J. C. (2002) Linkage of multiequilibria in DNA recognition by the D53H Escherichia coli, cAMP receptor protein Biochemistry 41, 14935-14943
    • (2002) Biochemistry , vol.41 , pp. 14935-14943
    • Lin, S.H.1    Lee, J.C.2
  • 23
    • 0024844517 scopus 로고
    • Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site
    • Ebright, R. H., Ebright, Y. W., and Gunasekera, A. (1989) Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site Nucleic Acids Res. 17, 10295-10305
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10295-10305
    • Ebright, R.H.1    Ebright, Y.W.2    Gunasekera, A.3
  • 24
    • 0028023784 scopus 로고
    • Nucleic-Acid Modeling Tool (Namot): An Interactive Graphic Tool for Modeling Nucleic Acid Structures
    • Tung, C. S. and Carter, E. S. (1994) Nucleic-Acid Modeling Tool (Namot): An Interactive Graphic Tool for Modeling Nucleic Acid Structures Comput. Appl. Biosci. 10, 427-433
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 427-433
    • Tung, C.S.1    Carter, E.S.2
  • 25
    • 0028335423 scopus 로고
    • Fluorescence study on the nonspecific-binding of cyclic-AMP receptor protein to DNA: Effect of pH
    • Giraud-Panis, M. J., Toulme, F., Blazy, B., Maurizot, J. C., and Culard, F. (1994) Fluorescence study on the nonspecific-binding of cyclic-AMP receptor protein to DNA: Effect of pH Biochimie 76, 133-139
    • (1994) Biochimie , vol.76 , pp. 133-139
    • Giraud-Panis, M.J.1    Toulme, F.2    Blazy, B.3    Maurizot, J.C.4    Culard, F.5
  • 26
    • 0036786881 scopus 로고    scopus 로고
    • Communications between the high-affinity cyclic nucleotide binding sites in E. coli cyclic AMP receptor protein: Effect of single site mutations
    • Lin, S. H. and Lee, J. C. (2002) Communications between the high-affinity cyclic nucleotide binding sites in E. coli cyclic AMP receptor protein: Effect of single site mutations Biochemistry 41, 11857-11867
    • (2002) Biochemistry , vol.41 , pp. 11857-11867
    • Lin, S.H.1    Lee, J.C.2
  • 27
    • 0018798893 scopus 로고
    • Cooperative Binding to DNA of Catabolite Activator Protein of Escherichia coli
    • Saxe, S. A. and Revzin, A. (1979) Cooperative Binding to DNA of Catabolite Activator Protein of Escherichia coli Biochemistry 18, 255-263
    • (1979) Biochemistry , vol.18 , pp. 255-263
    • Saxe, S.A.1    Revzin, A.2
  • 28
    • 0018668914 scopus 로고
    • Non-specific Interactions of CRP from E. coli with native and denatured DNAs: Control of binding by cAMP and cGMP and by cation concentration
    • Takahashi, M., Blazy, B., and Baudras, A. (1979) Non-specific Interactions of CRP from E. coli with native and denatured DNAs: Control of binding by cAMP and cGMP and by cation concentration Nucleic Acids Res. 7, 1699-1712
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1699-1712
    • Takahashi, M.1    Blazy, B.2    Baudras, A.3
  • 29
    • 0024381106 scopus 로고
    • Ligand-Modulated Binding of a Gene Regulatory Protein to DNA: Quantitative Analysis of Cyclic-AMP Induced Binding of CRP from Escherichia coli to Non-Specific and Specific DNA Targets
    • Takahashi, M., Blazy, B., Baudras, A., and Hillen, W. (1989) Ligand-Modulated Binding of a Gene Regulatory Protein to DNA: Quantitative Analysis of Cyclic-AMP Induced Binding of CRP from Escherichia coli to Non-Specific and Specific DNA Targets J. Mol. Biol. 207, 783-796
    • (1989) J. Mol. Biol. , vol.207 , pp. 783-796
    • Takahashi, M.1    Blazy, B.2    Baudras, A.3    Hillen, W.4
  • 30
    • 0024462882 scopus 로고
    • Escherichia coli cAMP Receptor Protein: Evidence for 3 Protein Conformational States with Different Promoter Binding Affinities
    • Heyduk, T. and Lee, J. C. (1989) Escherichia coli cAMP Receptor Protein: Evidence for 3 Protein Conformational States with Different Promoter Binding Affinities Biochemistry 28, 6914-6924
    • (1989) Biochemistry , vol.28 , pp. 6914-6924
    • Heyduk, T.1    Lee, J.C.2
  • 31
    • 38949192898 scopus 로고    scopus 로고
    • Chemical linkage at allosteric activation of E. coli cAMP receptor protein
    • Tutar, Y. (2008) Chemical linkage at allosteric activation of E. coli cAMP receptor protein Protein J. 27, 21-29
    • (2008) Protein J. , vol.27 , pp. 21-29
    • Tutar, Y.1
  • 32
    • 0024295009 scopus 로고
    • Dynamics of Repressor Operator Recognition: The Tn10-Encoded Tetracycline Resistance Control
    • Kleinschmidt, C., Tovar, K., Hillen, W., and Porschke, D. (1988) Dynamics of Repressor Operator Recognition: The Tn10-Encoded Tetracycline Resistance Control Biochemistry 27, 1094-1104
    • (1988) Biochemistry , vol.27 , pp. 1094-1104
    • Kleinschmidt, C.1    Tovar, K.2    Hillen, W.3    Porschke, D.4
  • 33
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford, S. E. and Marko, J. F. (2004) How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 34
    • 0015894209 scopus 로고
    • Different Cyclic-AMP Requirements for Induction of Arabinose and Lactose Operons of Escherichia coli
    • Lis, J. T. and Schleif, R. (1973) Different Cyclic-AMP Requirements for Induction of Arabinose and Lactose Operons of Escherichia coli J. Mol. Biol. 79, 149-162
    • (1973) J. Mol. Biol. , vol.79 , pp. 149-162
    • Lis, J.T.1    Schleif, R.2
  • 35
    • 0000819850 scopus 로고
    • Adenosine 3′-5′-Cyclic Monophosphate as Mediator of Catabolite Repression in Escherichia coli
    • Epstein, W., Rothmandenes, L. B., and Hesse, J. (1975) Adenosine 3′-5′-Cyclic Monophosphate as Mediator of Catabolite Repression in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 72, 2300-2304
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 2300-2304
    • Epstein, W.1    Rothmandenes, L.B.2    Hesse, J.3


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