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Volumn 290, Issue 1, 1999, Pages 37-48

DNA-induced conformational changes in cyclic AMP receptor protein: Detection and mapping by a protein footprinting technique using multiple chemical proteases

Author keywords

Conformational change; Cyclic AMP receptor protein; Protein footprinting; Protein DNA interactions

Indexed keywords

CYCLIC AMP; CYCLIC AMP BINDING PROTEIN; DNA; PROTEINASE; RNA POLYMERASE;

EID: 0033516613     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2858     Document Type: Article
Times cited : (19)

References (28)
  • 1
    • 0029202622 scopus 로고
    • Role of allosteric changes in cyclic AMP receptor protein function
    • Adhya S., Ryu S., Garges S. Role of allosteric changes in cyclic AMP receptor protein function. Subcell. Biochem. 24:1995;303-321.
    • (1995) Subcell. Biochem. , vol.24 , pp. 303-321
    • Adhya, S.1    Ryu, S.2    Garges, S.3
  • 2
    • 0021935421 scopus 로고
    • Effect of deoxyribose and ribopolymers on the sensitivity of cyclic-AMP receptor protein of Escherichia coli to proteolytic attack
    • Angulo J. A., Krakow J. S. Effect of deoxyribose and ribopolymers on the sensitivity of cyclic-AMP receptor protein of Escherichia coli to proteolytic attack. Arch. Biochem. Biophys. 236:1985;11-16.
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 11-16
    • Angulo, J.A.1    Krakow, J.S.2
  • 3
    • 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., Heyduk T. Mapping conformational changes in a protein:application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein. Biochemistry. 36:1997;10830-10836.
    • (1997) Biochemistry , vol.36 , pp. 10830-10836
    • Baichoo, N.1    Heyduk, T.2
  • 4
    • 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., Heyduk T. Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases. Protein Sci. 8:1999;518-528.
    • (1999) Protein Sci. , vol.8 , pp. 518-528
    • Baichoo, N.1    Heyduk, T.2
  • 6
    • 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
  • 8
    • 2642612817 scopus 로고    scopus 로고
    • Interactive and dominant effects of residues 128 and 141 on cyclic nucleotide and DNA bindings in Escherichia coli cAMP receptor protein
    • Cheng X., Lee J. C. Interactive and dominant effects of residues 128 and 141 on cyclic nucleotide and DNA bindings in Escherichia coli cAMP receptor protein. J. Biol. Chem. 273:1998;705-712.
    • (1998) J. Biol. Chem. , vol.273 , pp. 705-712
    • Cheng, X.1    Lee, J.C.2
  • 9
    • 0029118463 scopus 로고
    • Probing the mechanism of CRP activation by site-directed mutagenesis: The role of serine 128 in the allosteric pathway of cAMP receptor protein activation
    • Cheng X., Kovac L., Lee J. C. Probing the mechanism of CRP activation by site-directed mutagenesis: the role of serine 128 in the allosteric pathway of cAMP receptor protein activation. Biochemistry. 34:1995;10816-10826.
    • (1995) Biochemistry , vol.34 , pp. 10816-10826
    • Cheng, X.1    Kovac, L.2    Lee, J.C.3
  • 10
    • 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., Gunasekera A. 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. Nucl. Acids Res. 17:1989;10295-10305.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 10295-10305
    • Ebright, R.H.1    Ebright, Y.W.2    Gunasekera, A.3
  • 11
    • 0021972748 scopus 로고
    • Sites of allosteric shift in the structure of the cyclic AMP receptor protein
    • Garges S., Adhya S. Sites of allosteric shift in the structure of the cyclic AMP receptor protein. Cell. 41:1985;745-751.
    • (1985) Cell , vol.41 , pp. 745-751
    • Garges, S.1    Adhya, S.2
  • 12
    • 0023988001 scopus 로고
    • Cyclic AMP-induced conformational change of cyclic amp receptor protein (CRP): Intragenic suppressors of cyclic AMP-independent crp mutations
    • Garges S., Adhya S. Cyclic AMP-induced conformational change of cyclic amp receptor protein (CRP): intragenic suppressors of cyclic AMP-independent crp mutations. J. Bacteriol. 170:1988;1417-1422.
    • (1988) J. Bacteriol. , vol.170 , pp. 1417-1422
    • Garges, S.1    Adhya, S.2
  • 13
    • 0027931824 scopus 로고
    • Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach
    • Heyduk E., Heyduk T. Mapping protein domains involved in macromolecular interactions: a novel protein footprinting approach. Biochemistry. 33:1994;9643-9650.
    • (1994) Biochemistry , vol.33 , pp. 9643-9650
    • Heyduk, E.1    Heyduk, T.2
  • 14
    • 0029836226 scopus 로고    scopus 로고
    • Determinants of RNA polymerase alpha subunit for interaction with beta, beta', and sigma subunits: Hydroxyl-radical protein footprinting
    • Heyduk T., Heyduk E., Severinov K., Tang H., Ebright R. H. Determinants of RNA polymerase alpha subunit for interaction with beta, beta', and sigma subunits: hydroxyl-radical protein footprinting. Proc. Natl Acad. Sci. USA. 93:1996;10162-10166.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10162-10166
    • Heyduk, T.1    Heyduk, E.2    Severinov, K.3    Tang, H.4    Ebright, R.H.5
  • 16
    • 0026722419 scopus 로고
    • Allosteric changes in the cAMP receptor protein of Escherichia coli: Hinge reorientation
    • Kim J., Adhya S., Garges S. Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation. Proc. Natl Acad. Sci. USA. 89:1992;9700-9704.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9700-9704
    • Kim, J.1    Adhya, S.2    Garges, S.3
  • 17
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb A., Busby S., Buc H., Garges S., Adhya S. Transcriptional regulation by cAMP and its receptor protein. Annu. Rev. Biochem. 62:1993;749-795.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 749-795
    • Kolb, A.1    Busby, S.2    Buc, H.3    Garges, S.4    Adhya, S.5
  • 18
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin J. A., Yamamoto K. R. Allosteric effects of DNA on transcriptional regulators. Nature. 392:1998;885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 19
    • 0030582675 scopus 로고    scopus 로고
    • Transcription activation at class II CAP-dependent promoters: Two interactions between CAP and RNA polymerase
    • Niu W., Kim Y., Tau G., Heyduk T., Ebright R. H. Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase. Cell. 87:1996;1123-1134.
    • (1996) Cell , vol.87 , pp. 1123-1134
    • Niu, W.1    Kim, Y.2    Tau, G.3    Heyduk, T.4    Ebright, R.H.5
  • 20
    • 0030593510 scopus 로고    scopus 로고
    • Structure of the CAP-DNA complex at 2.5 Å resolution: A complete picture of the protein-DNA interface
    • Parkinson G., Wilson C., Gunasekera A., Ebright Y. W., Ebright R. E., Berman H. M. Structure of the CAP-DNA complex at 2.5 Å resolution: a complete picture of the protein-DNA interface. J. Mol. Biol. 260:1996;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
  • 21
    • 0000445736 scopus 로고    scopus 로고
    • The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer
    • Passner J. M., Steitz T. A. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc. Natl Acad. Sci. USA. 94:1997;2843-2847.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kda
    • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kda. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 23
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees
    • Schultz S. C., Shields G. C., Steitz T. A. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science. 253:1991;1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 24
    • 0026323540 scopus 로고
    • Nuclease activity of 1,10-phenanthroline-copper in study of protein-DNA interactions
    • Sigman D. S., Kuwabara M. D., Chen C. H., Bruice T. W. Nuclease activity of 1,10-phenanthroline-copper in study of protein-DNA interactions. Methods Enzymol. 208:1991;414-433.
    • (1991) Methods Enzymol. , vol.208 , pp. 414-433
    • Sigman, D.S.1    Kuwabara, M.D.2    Chen, C.H.3    Bruice, T.W.4
  • 25
    • 0025774847 scopus 로고
    • Single amino acid substitutions in the cAMP receptor protein specifically abolish regulation by the CytR repressor inEscherichia coli
    • Sogaard-Andersen L., Mironov A. S., Pedersen H., Sukhodelets V. V., Valentin-Hansen P. Single amino acid substitutions in the cAMP receptor protein specifically abolish regulation by the CytR repressor inEscherichia coli. Proc. Natl Acad Sci. USA. 88:1991;4921-4925.
    • (1991) Proc. Natl Acad Sci. USA , vol.88 , pp. 4921-4925
    • Sogaard-Andersen, L.1    Mironov, A.S.2    Pedersen, H.3    Sukhodelets, V.V.4    Valentin-Hansen, P.5
  • 26
    • 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 M.T., Jr.2
  • 27
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution
    • Weber I. T., Steitz T. A. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198:1987;311-326.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 28
    • 0027161386 scopus 로고
    • Identification of the activating region of catabolite gene activator protein (CAP): Isolation and characterization of mutants of CAP specifically defective in transcription activation
    • Zhou Y., Zhang X., Ebright R. H. Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation. Proc. Natl Acad. Sci. USA. 90:1993;6081-6085.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6081-6085
    • Zhou, Y.1    Zhang, X.2    Ebright, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.