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Volumn 292, Issue 3, 1999, Pages 619-632

Ligand-linked structural changes in the Escherichia coli biotin repressor: The significance of surface loops for binding and allostery

Author keywords

Allostery; Ligand binding; Protein footprinting; Surface loops

Indexed keywords

ADENOSINE TRIPHOSPHATE; APOLIPOPROTEIN B; BACTERIAL DNA; BIOTIN; DNA BINDING PROTEIN; HYBRID PROTEIN; HYDROXYL RADICAL; SYNTHETASE;

EID: 0033600802     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3086     Document Type: Article
Times cited : (32)

References (39)
  • 1
    • 0027431496 scopus 로고
    • Cooperative binding of the repressor of biotin biosynthesis to the biotin operator
    • Abbott J., Beckett D. Cooperative binding of the repressor of biotin biosynthesis to the biotin operator. Biochemistry. 32:1993;9649-9656.
    • (1993) Biochemistry , vol.32 , pp. 9649-9656
    • Abbott, J.1    Beckett, D.2
  • 2
    • 0030870810 scopus 로고    scopus 로고
    • Mapping conformational changes in a protein: Application of protein footprinting technique to cAMP-induced conformational changes of cAMP receptor protein (CRP)
    • Baichoo N., Heyduk T. Mapping conformational changes in a protein: application of protein footprinting technique to cAMP-induced conformational changes of cAMP receptor protein (CRP). Biochemistry. 36:1997;10830-10836.
    • (1997) Biochemistry , vol.36 , pp. 10830-10836
    • Baichoo, N.1    Heyduk, T.2
  • 3
    • 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
  • 4
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • Barker D. F., Campbell A. M. The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase. J. Mol. Biol. 146:1981;451-467.
    • (1981) J. Mol. Biol. , vol.146 , pp. 451-467
    • Barker, D.F.1    Campbell, A.M.2
  • 5
    • 0022437260 scopus 로고
    • Quantitative DNase I footprint titration: A method for studying protein-DNA interactions
    • Brenowitz M., Senear D. F., Shea M. A., Ackers G. K. Quantitative DNase I footprint titration: a method for studying protein-DNA interactions. Methods. Enzymol. 130:1986;133-181.
    • (1986) Methods. Enzymol. , vol.130 , pp. 133-181
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 6
    • 0022535750 scopus 로고
    • DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli
    • Buoncristiani M. R., Howard P. K., Otsuka A. J. DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli. Gene. 44:1986;255-261.
    • (1986) Gene , vol.44 , pp. 255-261
    • Buoncristiani, M.R.1    Howard, P.K.2    Otsuka, A.J.3
  • 8
    • 0025262186 scopus 로고
    • In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: Cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino acid sequence
    • Crimmins D. L., McCourt D. W., Thoma R. S., Scott M. G., Macke K., Schwartz B. D. In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino acid sequence. Anal. Biochem. 187:1990;27-38.
    • (1990) Anal. Biochem. , vol.187 , pp. 27-38
    • Crimmins, D.L.1    McCourt, D.W.2    Thoma, R.S.3    Scott, M.G.4    MacKe, K.5    Schwartz, B.D.6
  • 9
    • 0024349661 scopus 로고
    • The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme
    • Cronan J. E. Jr. The E. coli bio operon: transcriptional repression by an essential protein modification enzyme. Cell. 58:1989;427-429.
    • (1989) Cell , vol.58 , pp. 427-429
    • Cronan J.E., Jr.1
  • 11
    • 0032830564 scopus 로고    scopus 로고
    • Dimerization of the Escherichia coli biotin repressor: Corepressor function in protein assembly
    • Eisenstein E., Beckett D. Dimerization of the Escherichia coli biotin repressor: corepressor function in protein assembly. Biochemistry. In the press:1999.
    • (1999) Biochemistry
    • Eisenstein, E.1    Beckett, D.2
  • 12
    • 0028338864 scopus 로고
    • Structure and energy change in hemoglobin by hydrogen exchange labeling
    • Englander S. W., Englander J. J. Structure and energy change in hemoglobin by hydrogen exchange labeling. Methods Enzymol. 232:1994;26-42.
    • (1994) Methods Enzymol. , vol.232 , pp. 26-42
    • Englander, S.W.1    Englander, J.J.2
  • 13
    • 0028096754 scopus 로고
    • Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues
    • Ermacora M. R., Ledman D. W., Hellinga H. W., Hsu G. W., Fox R. O. Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues. Biochemistry. 33:1994;13625-13641.
    • (1994) Biochemistry , vol.33 , pp. 13625-13641
    • ErMacOra, M.R.1    Ledman, D.W.2    Hellinga, H.W.3    Hsu, G.W.4    Fox, R.O.5
  • 14
    • 0029664584 scopus 로고    scopus 로고
    • Binding of the σ70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting
    • Greiner D. P., Hughes K. A., Gunasekera A. H., Meares C. H. Binding of the σ70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting. Proc. Natl Acad. Sci. USA. 93:1996;71-75.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 71-75
    • Greiner, D.P.1    Hughes, K.A.2    Gunasekera, A.H.3    Meares, C.H.4
  • 15
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison C. J., Bohm A. A., Nelson H. C. M. Crystal structure of the DNA binding domain of the heat shock transcription factor. Nature. 263:1994;224-227.
    • (1994) Nature , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 16
    • 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
  • 17
    • 0029836226 scopus 로고    scopus 로고
    • Determinants of RNA polymerase α subunit for interaction with β, β′ and σ subunits: Hydroxyl-radical protein footprinting
    • Heyduk T., Heyduk E., Severinov K., Tang H., Ebright R. H. Determinants of RNA polymerase α subunit for interaction with β, β′ and σ 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
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromoleculer structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromoleculer structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 19
    • 0001453814 scopus 로고
    • The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+) biotin. II. Investigation of the reaction mechanism
    • Lane M. D., Rominger K. L., Young D. L., Lynen F. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+) biotin. II. Investigation of the reaction mechanism. J. Biol. Chem. 239:1964;2865-2871.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2865-2871
    • Lane, M.D.1    Rominger, K.L.2    Young, D.L.3    Lynen, F.4
  • 20
    • 0024359787 scopus 로고
    • Defining the inside and outside of a catalytic RNA molecule
    • Latham J. A., Cech T. R. Defining the inside and outside of a catalytic RNA molecule. Science. 245:1989;276-282.
    • (1989) Science , vol.245 , pp. 276-282
    • Latham, J.A.1    Cech, T.R.2
  • 23
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handedB -DNA
    • McKay D. B., Steitz T. A. Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handedB -DNA. Nature. 290:1981;744-749.
    • (1981) Nature , vol.290 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 25
    • 0018162576 scopus 로고
    • The regulatory region of the biotin operon in Escherichia coli
    • Otsuka A. J., Abelson J. The regulatory region of the biotin operon in Escherichia coli. Nature. 276:1978;689-693.
    • (1978) Nature , vol.276 , pp. 689-693
    • Otsuka, A.J.1    Abelson, J.2
  • 26
  • 28
    • 0018538322 scopus 로고
    • Biotinyl 5′- adenylate: Corepressor role in the regulation of the biotin genes of Escherichia coli K-12
    • Prakash O., Eisenberg M. A. Biotinyl 5′- adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12. Proc. Natl Acad. Sci. USA. 76:1979;5592-5595.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 5592-5595
    • Prakash, O.1    Eisenberg, M.A.2
  • 29
    • 0032512423 scopus 로고    scopus 로고
    • Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1
    • Reising K. A., Ahn N. G. Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1. Biochemistry. 37:1998;463-475.
    • (1998) Biochemistry , vol.37 , pp. 463-475
    • Reising, K.A.1    Ahn, N.G.2
  • 31
    • 0023472472 scopus 로고
    • Tricine-dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., von Jagow G. Tricine-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
    • Schägger, H.1    Von Jagow, G.2
  • 32
    • 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
  • 33
    • 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., Beckett D. Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex. Biochemistry. 37:1998a;3210-3219.
    • (1998) Biochemistry , vol.37 , pp. 3210-3219
    • Streaker, E.D.1    Beckett, D.2
  • 34
    • 0032525244 scopus 로고    scopus 로고
    • A map of the biotin repressor-biotin operator interface: Binding of a winged helix-turn-helix protein dimer to a 40 base-pair site
    • Streaker E. D., Beckett D. A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a 40 base-pair site. J. Mol. Biol. 278:1998b;787-800.
    • (1998) J. Mol. Biol. , vol.278 , pp. 787-800
    • Streaker, E.D.1    Beckett, D.2
  • 35
    • 0030906456 scopus 로고    scopus 로고
    • Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arbidopsis thaliana: Subcellular fractionation studies and isolation of a cDNA clone
    • Tissot G., Douce R., Alban C. Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arbidopsis thaliana: subcellular fractionation studies and isolation of a cDNA clone. Biochem. J. 323:1997;179-188.
    • (1997) Biochem. J. , vol.323 , pp. 179-188
    • Tissot, G.1    Douce, R.2    Alban, C.3
  • 36
    • 0026666377 scopus 로고
    • The E. coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin and DNA-binding domains
    • Wilson K. P., Shewchuk L. M., Brennan R. G., Otsuka A. J., Matthews B. W. The E. coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin and DNA-binding domains. Proc. Natl Acad. Sci. USA. 89:1992;9257-9261.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 37
    • 0030060228 scopus 로고    scopus 로고
    • Evidence for inter-domain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant
    • Xu Y., Beckett D. Evidence for inter-domain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Biochemistry. 35:1996;1783-1792.
    • (1996) Biochemistry , vol.35 , pp. 1783-1792
    • Xu, Y.1    Beckett, D.2
  • 38
    • 0029565346 scopus 로고
    • Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis
    • Xu Y., Nenortas E., Beckett D. Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. Biochemistry. 34:1995;16624-16631.
    • (1995) Biochemistry , vol.34 , pp. 16624-16631
    • Xu, Y.1    Nenortas, E.2    Beckett, D.3
  • 39
    • 0029918874 scopus 로고    scopus 로고
    • Thermodynamic analysis of binding of the Escherichia coli repressor of biotin biosynthesis to small ligands
    • Xu Y., Johnson C. R., Beckett D. Thermodynamic analysis of binding of the Escherichia coli repressor of biotin biosynthesis to small ligands. Biochemistry. 35:1996;5509-5517.
    • (1996) Biochemistry , vol.35 , pp. 5509-5517
    • Xu, Y.1    Johnson, C.R.2    Beckett, D.3


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