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Volumn 45, Issue 45, 2006, Pages 13438-13446

CRP subunit association and hinge conformation changes in response to cAMP binding: Analysis of C-helix cysteine-substituted CRP

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CHEMICAL BONDS; COMPLEXATION; CONFORMATIONS; DIMERS; SUBSTITUTION REACTIONS;

EID: 33750982725     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0610855     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 7444245668 scopus 로고    scopus 로고
    • Identification of the CRP regulon using in vitro and in vivo transcriptional profiling
    • Zheng, D., 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.1    Constantinidou, C.2    Hobman, J.L.3    Minchin, S.D.4
  • 2
    • 0035810698 scopus 로고    scopus 로고
    • Allosteric regulation of the cAMP receptor protein
    • Harman, J. G. (2001) Allosteric regulation of the cAMP receptor protein, Biochim. Biophys. Acta 1547, 1-17.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 1-17
    • Harman, J.G.1
  • 3
    • 0020490340 scopus 로고
    • Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein
    • Aiba, H., Fujimoto, S., and Ozaki, N. (1982) Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein, Nucleic Acids Res. 10, 1345-1362.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1345-1362
    • Aiba, H.1    Fujimoto, S.2    Ozaki, N.3
  • 4
    • 0020490341 scopus 로고
    • Cloning and sequence of the crp gene of Escherichia coli K 12
    • Cossart, P., and Gicquel-Sanzey, B. (1982) Cloning and sequence of the crp gene of Escherichia coli K 12, Nucleic Acids Res. 10, 1363-1378.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1363-1378
    • Cossart, P.1    Gicquel-Sanzey, B.2
  • 5
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5Å resolution
    • Weber, I.T., and Steitz, T. A. (1987) Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5Å resolution, J. Mol. Biol. 198, 311-326.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 6
    • 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
  • 7
    • 0024462882 scopus 로고
    • Escherichia coli cAMP receptor protein: Evidence for three protein conformational states with different promoter binding affinities
    • Heyduk, T., and Lee, J.C. (1989) Escherichia coli cAMP receptor protein: evidence for three 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
  • 8
    • 0024412668 scopus 로고
    • Modulation of the stability of a gene-regulatory protein dimer by DNA and cAMP
    • Brown, A. M., and Crothers, D. M. (1989) Modulation of the stability of a gene-regulatory protein dimer by DNA and cAMP, Proc. Natl. Acad. Sci. U.S.A. 86, 7387-7391.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7387-7391
    • Brown, A.M.1    Crothers, D.M.2
  • 9
    • 0027162425 scopus 로고
    • Energetics of intersubunit and intrasubunit interactions of Escherichia coli adenosine cyclic 3′,5′-phosphate receptor protein
    • Cheng, X., Gonzalez, M. L., and Lee, J. C. (1993) Energetics of intersubunit and intrasubunit interactions of Escherichia coli adenosine cyclic 3′,5′-phosphate receptor protein, Biochemistry 32, 8130-1839.
    • (1993) Biochemistry , vol.32 , pp. 8130-11839
    • Cheng, X.1    Gonzalez, M.L.2    Lee, J.C.3
  • 10
    • 0017803253 scopus 로고
    • Production and properties of the alpha core derived from the cyclic adenosine monophosphate receptor protein of Escherichia coli
    • Eilen, E., Pampeno, C., and Krakow, J. S. (1978) Production and properties of the alpha core derived from the cyclic adenosine monophosphate receptor protein of Escherichia coli, Biochemistry 17, 2469-2473.
    • (1978) Biochemistry , vol.17 , pp. 2469-2473
    • Eilen, E.1    Pampeno, C.2    Krakow, J.S.3
  • 11
    • 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
  • 12
    • 0027327859 scopus 로고
    • CAP interacts with RNA polymerase in solution in the absence of promoter DNA
    • Heyduk, T., Lee, J. C., Ebright, Y. W., Blatter, E. E., Zhou, Y., and Ebright, R. H. (1993) CAP interacts with RNA polymerase in solution in the absence of promoter DNA, Nature 364, 548-549.
    • (1993) Nature , vol.364 , pp. 548-549
    • Heyduk, T.1    Lee, J.C.2    Ebright, Y.W.3    Blatter, E.E.4    Zhou, Y.5    Ebright, R.H.6
  • 13
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby, S., and Ebright, R. H. (1999) Transcription activation by catabolite activator protein (CAP), J. Mol. Biol. 293, 199-213.
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 14
    • 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
  • 15
    • 0034671172 scopus 로고    scopus 로고
    • Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1Å resolution
    • Passner, J. M., Schultz, S. C., and Steitz, T. A. (2000) Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1Å resolution, J. Mol. Biol. 304, 847-859.
    • (2000) J. Mol. Biol. , vol.304 , pp. 847-859
    • Passner, J.M.1    Schultz, S.C.2    Steitz, T.A.3
  • 16
    • 20544478449 scopus 로고    scopus 로고
    • Proposed structural mechanism of Escherichia coli cAMP receptor protein cAMP-dependent proteolytic protection and selective and non-selective DNA binding
    • Scott, S.-P., and Jarjous, S. (2005) Proposed structural mechanism of Escherichia coli cAMP receptor protein cAMP-dependent proteolytic protection and selective and non-selective DNA binding, Biochemistry 44, 8730-8748.
    • (2005) Biochemistry , vol.44 , pp. 8730-8748
    • Scott, S.-P.1    Jarjous, S.2
  • 17
    • 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
  • 18
    • 0030870810 scopus 로고    scopus 로고
    • Mapping conformational changes in a protein: Application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein
    • Baichoo, N., and Heyduk, T. (1997) Mapping conformational changes in a protein: application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein, Biochemistry 36, 10830-10836.
    • (1997) Biochemistry , vol.36 , pp. 10830-10836
    • Baichoo, N.1    Heyduk, T.2
  • 19
    • 0032980418 scopus 로고    scopus 로고
    • Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases
    • Baichoo, N., and Heyduk, T. (1999) Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases, Protein Sci. 8, 518-528.
    • (1999) Protein Sci. , vol.8 , pp. 518-528
    • Baichoo, N.1    Heyduk, T.2
  • 20
    • 0034649356 scopus 로고    scopus 로고
    • Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding
    • Won, H.-S., Yamazaki, T., Lee, T.-W., Yoon, M.-K., Park, S.-H., Otomo, T., Kyogoku, Y., and Lee, B.-J. (2000) Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding, Biochemistry 39, 13953-13962.
    • (2000) Biochemistry , vol.39 , pp. 13953-13962
    • Won, H.-S.1    Yamazaki, T.2    Lee, T.-W.3    Yoon, M.-K.4    Park, S.-H.5    Otomo, T.6    Kyogoku, Y.7    Lee, B.-J.8
  • 21
    • 0021972748 scopus 로고
    • Sites of allosteric shift in the structure of the cyclic AMP receptor protein
    • Garges, S., and Adhya, S. (1985) Sites of allosteric shift in the structure of the cyclic AMP receptor protein, Cell 41, 745-751.
    • (1985) Cell , vol.41 , pp. 745-751
    • Garges, S.1    Adhya, S.2
  • 22
    • 0027941670 scopus 로고
    • Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: Targeting positions 83,127 and 128 of the cyclic nucleotide binding pocket
    • Lee, E. J., Glasgow, J., Leu, S.-F., Beldluz, A. O., and Harman, J. G. (1994) Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 83,127 and 128 of the cyclic nucleotide binding pocket, Nucleic Acids Res. 22, 2894-2901.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2894-2901
    • Lee, E.J.1    Glasgow, J.2    Leu, S.-F.3    Beldluz, A.O.4    Harman, J.G.5
  • 23
    • 0022902508 scopus 로고
    • Structure-function analysis of three cAMP-independent forms of the cAMP receptor protein
    • Harman, J. G., Peterkofsky, A., and McKenney, K. (1986) Structure-function analysis of three cAMP-independent forms of the cAMP receptor protein, J. Biol. Chem. 261, 16332-16339.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16332-16339
    • Harman, J.G.1    Peterkofsky, A.2    McKenney, K.3
  • 24
    • 0018598323 scopus 로고
    • L to promote gene expression in hybrid plasmid cloning vehicles
    • L to promote gene expression in hybrid plasmid cloning vehicles, Methods Enzymol. 68, 482-493.
    • (1979) Methods Enzymol. , vol.68 , pp. 482-493
    • Bernard, H.-D.1    Helinski, D.R.2
  • 25
    • 0027155860 scopus 로고
    • Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: Targeting positions 72 and 82 of the cyclic nucleotide binding pocket
    • Belduz, A. O., Lee, E. J., and Harman, J. G. (1993) Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 72 and 82 of the cyclic nucleotide binding pocket, Nucleic Acids Res. 21, 1827-1835.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1827-1835
    • Belduz, A.O.1    Lee, E.J.2    Harman, J.G.3
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972) Experiments in Molecular Genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 28
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton, J. M. (1981) Disulphide bridges in globular proteins, J. Mol. Biol. 151, 261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 29
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981) The anatomy and taxonomy of protein structure, Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 30
    • 0021199710 scopus 로고
    • Disulfide bond formation in proteins
    • Creighton, T. E. (1984) Disulfide bond formation in proteins, Methods Enzymol. 107, 305-329.
    • (1984) Methods Enzymol. , vol.107 , pp. 305-329
    • Creighton, T.E.1
  • 31
    • 0033545897 scopus 로고    scopus 로고
    • Position 127 amino acid substitutions affect the formation of CRP:cAMP:lacP complexes but not CRP:cAMP:RNA polymerase complexes at lacP
    • Leu, S.-F., Baker, C. H., Lee, E. J., and Harman, J. G. (1999) Position 127 amino acid substitutions affect the formation of CRP: cAMP:lacP complexes but not CRP:cAMP:RNA polymerase complexes at lacP, Biochemistry 38, 6222-6230.
    • (1999) Biochemistry , vol.38 , pp. 6222-6230
    • Leu, S.-F.1    Baker, C.H.2    Lee, E.J.3    Harman, J.G.4
  • 32
    • 0016607902 scopus 로고
    • Cyclic adenosine monophosphate receptor: Effect of cyclic AMP analogues on DNA binding and proteolytic inactivation
    • Krakow, J. (1975) Cyclic adenosine monophosphate receptor: effect of cyclic AMP analogues on DNA binding and proteolytic inactivation, Biochim. Biophys. Acta 383, 345-350.
    • (1975) Biochim. Biophys. Acta , vol.383 , pp. 345-350
    • Krakow, J.1
  • 33
    • 0026055297 scopus 로고
    • Nuclear magnetic resonance study on the structure and interaction of cyclic AMP receptor protein and its mutants: A deuterium-labeling and photo-CIDNP study
    • Lee, B.-J., Aiba, H., and Kyogoku, Y. (1991) Nuclear magnetic resonance study on the structure and interaction of cyclic AMP receptor protein and its mutants: a deuterium-labeling and photo-CIDNP study, Biochemistry 30, 9047-9054.
    • (1991) Biochemistry , vol.30 , pp. 9047-9054
    • Lee, B.-J.1    Aiba, H.2    Kyogoku, Y.3
  • 34
    • 0037426329 scopus 로고    scopus 로고
    • Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery
    • Tomlinson, S. R., Tutar, Y., and Harman, J. G. (2003) Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery, Biochemistry 42, 3759-3765.
    • (2003) Biochemistry , vol.42 , pp. 3759-3765
    • Tomlinson, S.R.1    Tutar, Y.2    Harman, J.G.3


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