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Volumn 15, Issue 6, 2005, Pages 1392-1396

Stability and structural change of cAMP receptor protein at low and high cAMP concentrations

Author keywords

cAMP receptor protein; Melting temperature; Protein stability

Indexed keywords

CYCLIC AMP; CYCLIC AMP BINDING PROTEIN; CYCLIC NUCLEOTIDE; MUTANT PROTEIN;

EID: 33646723476     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (24)
  • 1
    • 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., E. J. Lee, and J. G. Harman. 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
  • 2
    • 0024412668 scopus 로고
    • Modulation of the stability of a gene-regulatory protein dimer by DNA and CAMP
    • Brown, A. M. and D. M. Crothers. 1989. Modulation of the stability of a gene-regulatory protein dimer by DNA and CAMP. Proc. Natl. Acad. Sci. USA 86: 7387-7391.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7387-7391
    • Brown, A.M.1    Crothers, D.M.2
  • 3
    • 0028465007 scopus 로고
    • Identification of the target of a transcription activator protein by protein-protein photocrosslinking
    • Chen, Y., Y. W. Ebright, and R. H. Ebright. 1994. Identification of the target of a transcription activator protein by protein-protein photocrosslinking. Science 265: 90-92.
    • (1994) Science , vol.265 , pp. 90-92
    • Chen, Y.1    Ebright, Y.W.2    Ebright, R.H.3
  • 4
    • 0021245317 scopus 로고
    • Cyclic AMP receptor protein: Role in transcription activation
    • deCrombrugghe, B., S. Busby, and H. Buc. 1984. Cyclic AMP receptor protein: Role in transcription activation. Science 224: 831-838.
    • (1984) Science , vol.224 , pp. 831-838
    • deCrombrugghe, B.1    Busby, S.2    Buc, H.3
  • 5
    • 4444244079 scopus 로고    scopus 로고
    • Measurement of DNA helical change for the binding of cyclic AMP receptor protein to lac DNA
    • Gang, J. B. 2004. Measurement of DNA helical change for the binding of cyclic AMP receptor protein to lac DNA. Biochem. Biophys. Res. Commun. 322: 993-997.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 993-997
    • Gang, J.B.1
  • 6
    • 0021972748 scopus 로고
    • Sites of allosteric shift in the structure of the cyclic AMP receptor protein
    • Garges, S. and S. Adhya. 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
  • 7
    • 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
  • 8
    • 0023918854 scopus 로고
    • Arginine substituted for leucine at position 195 produces a cyclic AMP-independent form of the Escherichia coli cyclic AMP receptor protein
    • Harman, J. G., A. Peterkofsky, and K. McKenney. 1988. Arginine substituted for leucine at position 195 produces a cyclic AMP-independent form of the Escherichia coli cyclic AMP receptor protein. J. Biol. Chem. 263: 8072-8077.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8072-8077
    • Harman, J.G.1    Peterkofsky, A.2    McKenney, K.3
  • 9
    • 0026660254 scopus 로고
    • Global conformational changes in allosteric proteins
    • Heyduk, E., T. Heyduk, and J. C. Lee. 1992. Global conformational changes in allosteric proteins. J. Biol. Chem. 267: 3200-3204.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3200-3204
    • Heyduk, E.1    Heyduk, T.2    Lee, J.C.3
  • 10
  • 11
    • 0034708734 scopus 로고    scopus 로고
    • Kinetic studies of cAMP-induced allosteric changes in cyclic AMP receptor protein from Escherichia coli
    • Malecki, J., A. Polit, and Z. Wasylewski. 2000. Kinetic studies of cAMP-induced allosteric changes in cyclic AMP receptor protein from Escherichia coli. J. Biol. Chem. 275: 8480-8486.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8480-8486
    • Malecki, J.1    Polit, A.2    Wasylewski, Z.3
  • 12
    • 0032781898 scopus 로고    scopus 로고
    • Functional roles of the cyclic AMP-dependent forms of cyclic AMP receptor protein from Escherichia coli
    • Mukhopadhyay, J., R. Sur, and P. Parrack. 1999. Functional roles of the cyclic AMP-dependent forms of cyclic AMP receptor protein from Escherichia coli. FEBS Lett. 453: 215-218.
    • (1999) FEBS Lett. , vol.453 , pp. 215-218
    • Mukhopadhyay, J.1    Sur, R.2    Parrack, P.3
  • 13
    • 3242795070 scopus 로고    scopus 로고
    • Biochemical characterization of an ABC transporter gene involved in cephabacin biosynthesis in Lysobacter lactamgenus
    • Park, M. J., J. O. Yon, S. K. Lim, D. D. Ryu, and D. H. Nam. 2004. Biochemical characterization of an ABC transporter gene involved in cephabacin biosynthesis in Lysobacter lactamgenus. J. Microbiol. Biotechnol. 14: 635-638.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 635-638
    • Park, M.J.1    Yon, J.O.2    Lim, S.K.3    Ryu, D.D.4    Nam, D.H.5
  • 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 T. A. Steitz. 1997. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc. Natl. Acad. Sci. USA 94: 2843-2847.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 15
    • 0032515937 scopus 로고    scopus 로고
    • Escherichia coli cAMP receptor protein-DNA complexes. 1. Energetic contributions of half-sites and flanking sequences in DNA recognition
    • Pyles, E. A., A. J. Chin, and J. C. Lee. 1998. Escherichia coli cAMP receptor protein-DNA complexes. 1. Energetic contributions of half-sites and flanking sequences in DNA recognition. Biochemistry 37: 5194-5200.
    • (1998) Biochemistry , vol.37 , pp. 5194-5200
    • Pyles, E.A.1    Chin, A.J.2    Lee, J.C.3
  • 16
    • 0026499833 scopus 로고
    • Catabolite gene activator protein activation of lac transcription
    • Reznikoff, W. S. 1992. Catabolite gene activator protein activation of lac transcription. J. Bacteriol. 174: 655-658.
    • (1992) J. Bacteriol. , vol.174 , pp. 655-658
    • Reznikoff, W.S.1
  • 17
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method
    • Santoro, M. M. and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 18
    • 0034691250 scopus 로고    scopus 로고
    • Intersubunit association induces allosteric dependence of the T127L CRP mutant on PH
    • Shi, Y., S. Wang, and F. P. Schwarz. 2000. Intersubunit association induces allosteric dependence of the T127L CRP mutant on PH. Biochemistry 39: 7300-7308.
    • (2000) Biochemistry , vol.39 , pp. 7300-7308
    • Shi, Y.1    Wang, S.2    Schwarz, F.P.3
  • 20
    • 0032536817 scopus 로고    scopus 로고
    • A common role of CRP in transcription activation: CRP acts transiently to stimulate events leading to open complex formation at a diverse set of promoters
    • Tagami, H. and H. Aiba 1998. A common role of CRP in transcription activation: CRP acts transiently to stimulate events leading to open complex formation at a diverse set of promoters. EMBO J. 17: 1759-1767.
    • (1998) EMBO J. , vol.17 , pp. 1759-1767
    • Tagami, H.1    Aiba, H.2
  • 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., B. Blazy, and A. Baudras. 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
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution
    • Weber, I. T. and T. A. Steitz. 1987. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198: 311-326.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 23
    • 0346728561 scopus 로고    scopus 로고
    • Construction and characterization of multiple heavy metal-resistant phenol-degrading Pseudomonads strains
    • Yoon, K. P. 2003. Construction and characterization of multiple heavy metal-resistant phenol-degrading Pseudomonads strains. J. Microbiol. Biotechnol. 13: 1001-1007.
    • (2003) J. Microbiol. Biotechnol. , vol.13 , pp. 1001-1007
    • Yoon, K.P.1
  • 24
    • 0242636156 scopus 로고    scopus 로고
    • Purification and comparision of properties of the C-terminus truncated agarase of Pesudomonas sp. W7
    • Yoon, S.-C., J.-H. Lee, S.-H. Ahn, E.-M. Lee, E.-M. Park, and I.-S. Kong. 2003. Purification and comparision of properties of the C-terminus truncated agarase of Pesudomonas sp. W7. J. Microbiol. Biotechnol. 13: 767-772.
    • (2003) J. Microbiol. Biotechnol. , vol.13 , pp. 767-772
    • Yoon, S.-C.1    Lee, J.-H.2    Ahn, S.-H.3    Park, E.-M.4    Lee, E.-M.5    Kong, I.-S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.