메뉴 건너뛰기




Volumn 44, Issue 8, 2005, Pages 3112-3121

Use of binding enthalpy to drive an allosteric transition

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOSYNTHESIS; CALORIMETRY; CHEMICAL ACTIVATION; CHEMICAL BONDS; DIMERIZATION; DNA; ESCHERICHIA COLI; FREE ENERGY; MONOMERS; THERMODYNAMICS; TITRATION; VITAMINS;

EID: 14344255691     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047792k     Document Type: Article
Times cited : (31)

References (29)
  • 2
    • 0029093731 scopus 로고
    • Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers
    • Tao, X., Zeng, H. Y., and Murphy, J. R. (1995) Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers, Proc. Natl. Acad. Sci. U.S.A. 92, 6803-6807.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6803-6807
    • Tao, X.1    Zeng, H.Y.2    Murphy, J.R.3
  • 3
    • 0024349661 scopus 로고
    • The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme
    • Cronan, J. E., Jr. (1989) The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme, Cell 58, 427-429.
    • (1989) Cell , vol.58 , pp. 427-429
    • Cronan Jr., J.E.1
  • 4
    • 0019473758 scopus 로고
    • Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
    • Barker, D. F., and Campbell, A. M. (1981) Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli, J. Mol. Biol. 146, 469-492.
    • (1981) J. Mol. Biol. , vol.146 , pp. 469-492
    • Barker, D.F.1    Campbell, A.M.2
  • 5
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • Barker, D. F., and Campbell, A. M. (1981) The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase, J. Mol. Biol. 146, 451-461.
    • (1981) J. Mol. Biol. , vol.146 , pp. 451-461
    • Barker, D.F.1    Campbell, A.M.2
  • 6
    • 0001453814 scopus 로고
    • The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin
    • Lane, M. D., Rominger, K. L., Young, D. L., and Lynen, F. (1964) The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin, J. Biol. Chem. 239, 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
  • 7
    • 0018162576 scopus 로고
    • The regulatory region of the biotin operon in Escherichia coli
    • Otsuka, A., and Abelson, J. (1978) The regulatory region of the biotin operon in Escherichia coli, Nature 276, 689-694.
    • (1978) Nature , vol.276 , pp. 689-694
    • Otsuka, A.1    Abelson, J.2
  • 8
    • 0018538322 scopus 로고
    • Biotinyl 5′-adenylate: Corepressor role in the regulation of the biotin genes of Escherichia coli k-12
    • Prakash, O., and Eisenberg, M. A. (1979) Biotinyl 5′-adenylate: Corepressor role in the regulation of the biotin genes of Escherichia coli k-12, Proc. Natl. Acad. Sci. U.S.A. 76, 5592-5595.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 5592-5595
    • Prakash, O.1    Eisenberg, M.A.2
  • 9
    • 0026666377 scopus 로고
    • Escherichia 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., and Matthews, B. W. (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains, Proc. Natl. Acad. Sci. U.S.A. 89, 9257-9261.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 10
    • 0027431496 scopus 로고
    • Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence
    • Abbott, J., and Beckett, D. (1993) Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence, Biochemistry 32, 9649-9656.
    • (1993) Biochemistry , vol.32 , pp. 9649-9656
    • Abbott, J.1    Beckett, D.2
  • 11
    • 0032830564 scopus 로고    scopus 로고
    • Dimerization of the Escherichia coli biotin repressor: Corepressor function in protein assembly
    • Eisenstein, E., and Beckett, D. (1999) Dimerization of the Escherichia coli biotin repressor: Corepressor function in protein assembly, Biochemistry 38, 13077-13084.
    • (1999) Biochemistry , vol.38 , pp. 13077-13084
    • Eisenstein, E.1    Beckett, D.2
  • 12
    • 0037016018 scopus 로고    scopus 로고
    • The biotin repressor: Thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding
    • Streaker, E. D., Gupta, A., and Beckett, D. (2002) The biotin repressor: Thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding, Biochemistry 41, 14263-14271.
    • (2002) Biochemistry , vol.41 , pp. 14263-14271
    • Streaker, E.D.1    Gupta, A.2    Beckett, D.3
  • 13
    • 0034671258 scopus 로고    scopus 로고
    • Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor
    • Kwon, K., Streaker, E. D., Ruparelia, S., and Beckett, D. (2000) Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor, J. Mol. Biol. 304, 821-833.
    • (2000) J. Mol. Biol. , vol.304 , pp. 821-833
    • Kwon, K.1    Streaker, E.D.2    Ruparelia, S.3    Beckett, D.4
  • 14
    • 0037474538 scopus 로고    scopus 로고
    • Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding
    • Streaker, E. D., and Beckett, D. (2003) Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding, J. Mol. Biol. 325, 937-948.
    • (2003) J. Mol. Biol. , vol.325 , pp. 937-948
    • Streaker, E.D.1    Beckett, D.2
  • 15
    • 0035932977 scopus 로고    scopus 로고
    • Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator
    • Weaver, L. H., Kwon, K., Beckett, D., and Matthews, B. W. (2001) Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator, Proc. Natl. Acad. Sci. U.S.A. 98, 6045-6050.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6045-6050
    • Weaver, L.H.1    Kwon, K.2    Beckett, D.3    Matthews, B.W.4
  • 16
    • 1642384541 scopus 로고    scopus 로고
    • The biotin repressor: Modulation of allostery by corepressor analogs
    • Brown, P. H., Cronan, J. E., Grotli, M., and Beckett, D. (2004) The biotin repressor: Modulation of allostery by corepressor analogs, J. Mol. Biol. 337, 857-869.
    • (2004) J. Mol. Biol. , vol.337 , pp. 857-869
    • Brown, P.H.1    Cronan, J.E.2    Grotli, M.3    Beckett, D.4
  • 17
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • Sigurskjold, B. W. (2000) Exact analysis of competition ligand binding by displacement isothermal titration calorimetry, Anal. Biochem. 277, 260-266.
    • (2000) Anal. Biochem. , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 18
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce, M. M., Raman, C. S., and Nall, B. T. (1999) Isothermal titration calorimetry of protein-protein interactions, Methods 19, 213-221.
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 20
    • 0029565346 scopus 로고
    • Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis
    • Xu, Y., Nenortas, E., and Beckett, D. (1995) Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis, Biochemistry 34, 16624-16631.
    • (1995) Biochemistry , vol.34 , pp. 16624-16631
    • Xu, Y.1    Nenortas, E.2    Beckett, D.3
  • 21
    • 0027956678 scopus 로고
    • Thermodynamics of inhibitor binding to the catalytic site of glucoamylase from Aspergillus niger determined by displacement titration calorimetry
    • Sigurskjold, B. W., Berland, C. R., and Svensson, B. (1994) Thermodynamics of inhibitor binding to the catalytic site of glucoamylase from Aspergillus niger determined by displacement titration calorimetry, Biochemistry 33, 10191-10199.
    • (1994) Biochemistry , vol.33 , pp. 10191-10199
    • Sigurskjold, B.W.1    Berland, C.R.2    Svensson, B.3
  • 22
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov, I., and Bosshard, H. R. (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition, J. Mol. Recognit. 12, 3-18.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 23
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt, S., and Freire, E. (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry, Curr. Opin. Struct. Biol. 11, 560-566.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 24
    • 0035876257 scopus 로고    scopus 로고
    • The binding energetics of first- and second-generation hiv-1 protease inhibitors: Implications for drug design
    • Velazquez-Campoy, A., Kiso, Y., and Freire, E. (2001) The binding energetics of first- and second-generation hiv-1 protease inhibitors: Implications for drug design, Arch. Biochem. Biophys. 390, 169-175.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 169-175
    • Velazquez-Campoy, A.1    Kiso, Y.2    Freire, E.3
  • 25
    • 0029918874 scopus 로고    scopus 로고
    • Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis
    • Xu, Y., Johnson, C. R., and Beckett, D. (1996) Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis, Biochemistry 35, 5509-5517.
    • (1996) Biochemistry , vol.35 , pp. 5509-5517
    • Xu, Y.1    Johnson, C.R.2    Beckett, D.3
  • 26
    • 0026059557 scopus 로고
    • Calorimetric determination of cooperative interactions in high affinity binding processes
    • Bains, G., and Freire, E. (1991) Calorimetric determination of cooperative interactions in high affinity binding processes, Anal. Biochem. 192, 203-206.
    • (1991) Anal. Biochem. , vol.192 , pp. 203-206
    • Bains, G.1    Freire, E.2
  • 27
    • 2942557079 scopus 로고    scopus 로고
    • Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets
    • Ohtaka, H., Muzammil, S., Schon, A., Velazquez-Campoy, A., Vega, S., and Freire, E. (2004) Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets, Int. J. Biochem. Cell Biol. 36, 1787-1799.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1787-1799
    • Ohtaka, H.1    Muzammil, S.2    Schon, A.3    Velazquez-Campoy, A.4    Vega, S.5    Freire, E.6
  • 28
    • 0036176908 scopus 로고    scopus 로고
    • Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase
    • Kwon, K., Streaker, E. D., and Beckett, D. (2002) Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase, Protein Sci. 11, 558-570.
    • (2002) Protein Sci. , vol.11 , pp. 558-570
    • Kwon, K.1    Streaker, E.D.2    Beckett, D.3
  • 29
    • 0030060228 scopus 로고    scopus 로고
    • Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant
    • Xu, Y., and Beckett, D. (1996) Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant, Biochemistry 35, 1783-1792.
    • (1996) Biochemistry , vol.35 , pp. 1783-1792
    • Xu, Y.1    Beckett, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.