메뉴 건너뛰기




Volumn 376, Issue 2, 2008, Pages 466-481

Ligand-induced Conformational Changes and Conformational Dynamics in the Solution Structure of the Lactose Repressor Protein

Author keywords

allostery; LacI; small angle X ray scattering; solution structure

Indexed keywords

BACTERIAL PROTEIN; DIMER; DNA; HOMODIMER; LACTOSE REPRESSOR PROTEIN; LIGAND; UNCLASSIFIED DRUG;

EID: 38349193126     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.067     Document Type: Article
Times cited : (50)

References (77)
  • 1
    • 0018258345 scopus 로고
    • An amino-terminal fragment of lac repressor binds specifically to lac operator
    • Ogata R.T., and Gilbert W. An amino-terminal fragment of lac repressor binds specifically to lac operator. Proc. Natl. Acad. Sci. USA 75 (1978) 5851-5854
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5851-5854
    • Ogata, R.T.1    Gilbert, W.2
  • 2
    • 0015918916 scopus 로고
    • 2-terminal region and loss of the deoxyribonucleic acid-binding activity
    • 2-terminal region and loss of the deoxyribonucleic acid-binding activity. J. Biol. Chem. 248 (1973) 110-121
    • (1973) J. Biol. Chem. , vol.248 , pp. 110-121
    • Platt, T.1    Files, J.G.2    Weber, K.3
  • 3
    • 0029938053 scopus 로고    scopus 로고
    • Crystal structure of the lactose operon repressor and its complexes with DNA and inducer
    • Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C., Schumacher M.A., et al. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science 271 (1996) 1247-1254
    • (1996) Science , vol.271 , pp. 1247-1254
    • Lewis, M.1    Chang, G.2    Horton, N.C.3    Kercher, M.A.4    Pace, H.C.5    Schumacher, M.A.6
  • 4
    • 0035812627 scopus 로고    scopus 로고
    • Crystallographic analysis of Lac repressor bound to natural operator O1
    • Bell C.E., and Lewis M. Crystallographic analysis of Lac repressor bound to natural operator O1. J. Mol. Biol. 312 (2001) 921-926
    • (2001) J. Mol. Biol. , vol.312 , pp. 921-926
    • Bell, C.E.1    Lewis, M.2
  • 5
    • 0034089394 scopus 로고    scopus 로고
    • A closer view of the conformation of the Lac repressor bound to operator
    • Bell C.E., and Lewis M. A closer view of the conformation of the Lac repressor bound to operator. Nat. Struct. Biol. 7 (2000) 209-214
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 209-214
    • Bell, C.E.1    Lewis, M.2
  • 6
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to Gal and Lac repressors
    • Weickert M.J., and Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 267 (1992) 15869-15874
    • (1992) J. Biol. Chem. , vol.267 , pp. 15869-15874
    • Weickert, M.J.1    Adhya, S.2
  • 7
    • 0026723976 scopus 로고
    • Deletion of lactose repressor carboxyl-terminal domain affects tetramer formation
    • Chen J., and Matthews K.S. Deletion of lactose repressor carboxyl-terminal domain affects tetramer formation. J. Biol. Chem. 267 (1992) 13843-13850
    • (1992) J. Biol. Chem. , vol.267 , pp. 13843-13850
    • Chen, J.1    Matthews, K.S.2
  • 8
    • 0027297241 scopus 로고
    • Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4-helical bundle
    • Alberti S., Oehler S., von Wilcken-Bergmann B., and Müller-Hill B. Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4-helical bundle. EMBO J. 12 (1993) 3227-3236
    • (1993) EMBO J. , vol.12 , pp. 3227-3236
    • Alberti, S.1    Oehler, S.2    von Wilcken-Bergmann, B.3    Müller-Hill, B.4
  • 10
    • 0025343547 scopus 로고
    • The three operators of the lac operon cooperate in repression
    • Oehler S., Eismann E.R., Kramer H., and Müller-Hill B. The three operators of the lac operon cooperate in repression. EMBO J. 9 (1990) 973-979
    • (1990) EMBO J. , vol.9 , pp. 973-979
    • Oehler, S.1    Eismann, E.R.2    Kramer, H.3    Müller-Hill, B.4
  • 13
    • 0014966123 scopus 로고
    • lac repressor-operator interaction: II. Effect of galactosides and other ligands
    • Riggs A.D., Newby R.F., and Bourgeois S. lac repressor-operator interaction: II. Effect of galactosides and other ligands. J. Mol. Biol. 51 (1970) 303-314
    • (1970) J. Mol. Biol. , vol.51 , pp. 303-314
    • Riggs, A.D.1    Newby, R.F.2    Bourgeois, S.3
  • 14
    • 0015527295 scopus 로고
    • lac repressor-operator interaction: VI. The natural inducer of the lac operon
    • Jobe A., and Bourgeois S. lac repressor-operator interaction: VI. The natural inducer of the lac operon. J. Mol. Biol. 69 (1972) 397-408
    • (1972) J. Mol. Biol. , vol.69 , pp. 397-408
    • Jobe, A.1    Bourgeois, S.2
  • 15
    • 0016745534 scopus 로고
    • Interaction of effecting ligands with lac repressor and repressor-operator complex
    • Barkley M.D., Riggs A.D., Jobe A., and Burgeois S. Interaction of effecting ligands with lac repressor and repressor-operator complex. Biochemistry 14 (1975) 1700-1712
    • (1975) Biochemistry , vol.14 , pp. 1700-1712
    • Barkley, M.D.1    Riggs, A.D.2    Jobe, A.3    Burgeois, S.4
  • 16
    • 34249932435 scopus 로고    scopus 로고
    • Probing transcription factor dynamics at the single-molecule level in a living cell
    • Elf J., Li G.W., and Xie X.S. Probing transcription factor dynamics at the single-molecule level in a living cell. Science 316 (2007) 1191-1194
    • (2007) Science , vol.316 , pp. 1191-1194
    • Elf, J.1    Li, G.W.2    Xie, X.S.3
  • 17
    • 0016437021 scopus 로고
    • A comparison of lac repressor binding to operator and to nonoperator DNA
    • Lin S., and Riggs A.D. A comparison of lac repressor binding to operator and to nonoperator DNA. Biochem. Biophys. Res. Commun. 62 (1975) 704-710
    • (1975) Biochem. Biophys. Res. Commun. , vol.62 , pp. 704-710
    • Lin, S.1    Riggs, A.D.2
  • 18
    • 0016640172 scopus 로고
    • The general affinity of lac repressor for E. coli DNA: implications for gene regulation in procaryotes and eucaryotes
    • Lin S., and Riggs A.D. The general affinity of lac repressor for E. coli DNA: implications for gene regulation in procaryotes and eucaryotes. Cell 4 (1975) 107-111
    • (1975) Cell , vol.4 , pp. 107-111
    • Lin, S.1    Riggs, A.D.2
  • 19
    • 34249951731 scopus 로고    scopus 로고
    • Structural analysis of lac repressor bound to allosteric effectors
    • Daber R., Stayrook S., Rosenberg A., and Lewis M. Structural analysis of lac repressor bound to allosteric effectors. J. Mol. Biol. 370 (2007) 609-619
    • (2007) J. Mol. Biol. , vol.370 , pp. 609-619
    • Daber, R.1    Stayrook, S.2    Rosenberg, A.3    Lewis, M.4
  • 20
    • 0029004903 scopus 로고
    • Crystal structure of lac repressor core tetramer and its implications for DNA looping
    • Friedman A.M., Fischmann T.O., and Steitz T.A. Crystal structure of lac repressor core tetramer and its implications for DNA looping. Science 268 (1995) 1721-1727
    • (1995) Science , vol.268 , pp. 1721-1727
    • Friedman, A.M.1    Fischmann, T.O.2    Steitz, T.A.3
  • 21
    • 0027426159 scopus 로고
    • Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics
    • Chuprina V.P., Rullmann J.A., Lamerichs R.M., van Boom J.H., Boelens R., and Kaptein R. Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. J. Mol. Biol. 234 (1993) 446-462
    • (1993) J. Mol. Biol. , vol.234 , pp. 446-462
    • Chuprina, V.P.1    Rullmann, J.A.2    Lamerichs, R.M.3    van Boom, J.H.4    Boelens, R.5    Kaptein, R.6
  • 22
    • 0030596509 scopus 로고    scopus 로고
    • Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: change of tertiary structure upon binding to the lac operator
    • Slijper M., Bonvin A.M., Boelens R., and Kaptein R. Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: change of tertiary structure upon binding to the lac operator. J. Mol. Biol. 259 (1996) 761-773
    • (1996) J. Mol. Biol. , vol.259 , pp. 761-773
    • Slijper, M.1    Bonvin, A.M.2    Boelens, R.3    Kaptein, R.4
  • 23
    • 0037124326 scopus 로고    scopus 로고
    • Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain
    • Kalodimos C.G., Bonvin A.M., Salinas R.K., Wechselberger R., Boelens R., and Kaptein R. Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. EMBO J. 21 (2002) 2866-2876
    • (2002) EMBO J. , vol.21 , pp. 2866-2876
    • Kalodimos, C.G.1    Bonvin, A.M.2    Salinas, R.K.3    Wechselberger, R.4    Boelens, R.5    Kaptein, R.6
  • 25
    • 0033573062 scopus 로고    scopus 로고
    • The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator
    • Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R., and Kaptein R. The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator. Structure 7 (1999) 1483-1492
    • (1999) Structure , vol.7 , pp. 1483-1492
    • Spronk, C.A.1    Bonvin, A.M.2    Radha, P.K.3    Melacini, G.4    Boelens, R.5    Kaptein, R.6
  • 26
    • 0021143606 scopus 로고
    • Predicted structure of the sugar-binding site of the lac repressor
    • Sams C.F., Vyas N.K., Quiocho F.A., and Matthews K.S. Predicted structure of the sugar-binding site of the lac repressor. Nature 310 (1984) 429-430
    • (1984) Nature , vol.310 , pp. 429-430
    • Sams, C.F.1    Vyas, N.K.2    Quiocho, F.A.3    Matthews, K.S.4
  • 27
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J.H., Spolar R.S., and Record Jr. M.T. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209 (1989) 801-816
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.H.1    Spolar, R.S.2    Record Jr., M.T.3
  • 28
    • 0029976830 scopus 로고    scopus 로고
    • Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator
    • Spronk C.A.E.M., Slijper M., van Boom J.H., Kaptein R., and Boelens R. Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator. Nat. Struct. Biol. 3 (1996) 916-919
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 916-919
    • Spronk, C.A.E.M.1    Slijper, M.2    van Boom, J.H.3    Kaptein, R.4    Boelens, R.5
  • 29
    • 0035933104 scopus 로고    scopus 로고
    • Strong DNA binding by covalently linked dimeric Lac headpiece: evidence for the crucial role of the hinge helices
    • Kalodimos C.G., Folkers G.E., Boelens R., and Kaptein R. Strong DNA binding by covalently linked dimeric Lac headpiece: evidence for the crucial role of the hinge helices. Proc. Natl. Acad. Sci. USA 98 (2001) 6039-6044
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6039-6044
    • Kalodimos, C.G.1    Folkers, G.E.2    Boelens, R.3    Kaptein, R.4
  • 30
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., and Record Jr. M.T. 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 Jr., M.T.2
  • 31
    • 0028810684 scopus 로고
    • Mechanism of corepressor-mediated specific DNA binding by the purine repressor
    • Schumacher M.A., Choi K.Y., Lu F., Zalkin H., and Brennan R.G. Mechanism of corepressor-mediated specific DNA binding by the purine repressor. Cell 83 (1995) 147-155
    • (1995) Cell , vol.83 , pp. 147-155
    • Schumacher, M.A.1    Choi, K.Y.2    Lu, F.3    Zalkin, H.4    Brennan, R.G.5
  • 32
    • 0028334191 scopus 로고
    • Wild-type operator binding and altered cooperativity for inducer binding of lac repressor dimer mutant R3
    • Chen J., Alberti S., and Matthews K.S. Wild-type operator binding and altered cooperativity for inducer binding of lac repressor dimer mutant R3. J. Biol. Chem. 269 (1994) 12482-12487
    • (1994) J. Biol. Chem. , vol.269 , pp. 12482-12487
    • Chen, J.1    Alberti, S.2    Matthews, K.S.3
  • 33
    • 0023067531 scopus 로고
    • Lac repressor-Lac operator complexes. Solution X-ray scattering and electrophoretic studies
    • Culard F., Charlier M., Maurizot J.C., and Tardieu A. Lac repressor-Lac operator complexes. Solution X-ray scattering and electrophoretic studies. Eur. Biophys. J. 14 (1987) 169-178
    • (1987) Eur. Biophys. J. , vol.14 , pp. 169-178
    • Culard, F.1    Charlier, M.2    Maurizot, J.C.3    Tardieu, A.4
  • 34
    • 0019211990 scopus 로고
    • Small-angle X-ray studies of the quaternary structure of the lac repressor from Escherichia coli
    • Pilz I., Goral K., Kratky O., Bray R.P., Wade-Jardetzky N.G., and Jardetzky O. Small-angle X-ray studies of the quaternary structure of the lac repressor from Escherichia coli. Biochemistry 19 (1980) 4087-4090
    • (1980) Biochemistry , vol.19 , pp. 4087-4090
    • Pilz, I.1    Goral, K.2    Kratky, O.3    Bray, R.P.4    Wade-Jardetzky, N.G.5    Jardetzky, O.6
  • 35
    • 0019993652 scopus 로고
    • Escherichia coli lac repressor is elongated with its operator DNA binding domains located at both ends
    • McKay D.B., Pickover C.A., and Steitz T.A. Escherichia coli lac repressor is elongated with its operator DNA binding domains located at both ends. J. Mol. Biol. 156 (1982) 175-183
    • (1982) J. Mol. Biol. , vol.156 , pp. 175-183
    • McKay, D.B.1    Pickover, C.A.2    Steitz, T.A.3
  • 36
    • 0020854778 scopus 로고
    • Nonspecific binding of lac repressor to DNA. II. A small-angle neutron-scattering study
    • Charlier M., Maurizot J.C., and Zaccai G. Nonspecific binding of lac repressor to DNA. II. A small-angle neutron-scattering study. Biophys. Chem. 18 (1983) 313-322
    • (1983) Biophys. Chem. , vol.18 , pp. 313-322
    • Charlier, M.1    Maurizot, J.C.2    Zaccai, G.3
  • 37
    • 0019888622 scopus 로고
    • Neutron-scattering studies of lac repressor: a low-resolution model
    • Charlier M., Maurizot J.C., and Zaccai G. Neutron-scattering studies of lac repressor: a low-resolution model. J. Mol. Biol. 153 (1981) 177-182
    • (1981) J. Mol. Biol. , vol.153 , pp. 177-182
    • Charlier, M.1    Maurizot, J.C.2    Zaccai, G.3
  • 38
    • 0018967521 scopus 로고
    • Neutron scattering studies of lac repressor
    • Charlier M., Maurizot J.C., and Zaccai G. Neutron scattering studies of lac repressor. Nature 286 (1980) 423-425
    • (1980) Nature , vol.286 , pp. 423-425
    • Charlier, M.1    Maurizot, J.C.2    Zaccai, G.3
  • 40
    • 34347112128 scopus 로고
    • Die Roentgenkleinwinkel-Steuung von Dichtgepackten Kolloiden Systemen, I Teil
    • Porod G. Die Roentgenkleinwinkel-Steuung von Dichtgepackten Kolloiden Systemen, I Teil. Kolloid. Z. Biol. 124 (1951) 83-111
    • (1951) Kolloid. Z. Biol. , vol.124 , pp. 83-111
    • Porod, G.1
  • 41
    • 12544256134 scopus 로고    scopus 로고
    • Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly
    • Voss N.R., and Gerstein M. Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly. J. Mol. Biol. 346 (2005) 477-492
    • (2005) J. Mol. Biol. , vol.346 , pp. 477-492
    • Voss, N.R.1    Gerstein, M.2
  • 42
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.1
  • 43
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 44
    • 0026243243 scopus 로고
    • Mathematical methods in small-angle scattering data analysis
    • Svergun D.I. Mathematical methods in small-angle scattering data analysis. J. Appl. Crystallogr. 24 (1991) 485-492
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 485-492
    • Svergun, D.I.1
  • 45
    • 0001232884 scopus 로고
    • The small-angle approximation of X-ray and neutron scatter from rigid rods of non-uniform cross section of finite length
    • Hjelm R.J. The small-angle approximation of X-ray and neutron scatter from rigid rods of non-uniform cross section of finite length. J. Appl. Crystallogr. 18 (1985) 452-460
    • (1985) J. Appl. Crystallogr. , vol.18 , pp. 452-460
    • Hjelm, R.J.1
  • 46
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small_angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small_angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 47
    • 23944464891 scopus 로고    scopus 로고
    • Integrated insights from simulation, experiment, and mutational analysis yield new details of LacI function
    • Swint-Kruse L., Zhan H., and Matthews K.S. Integrated insights from simulation, experiment, and mutational analysis yield new details of LacI function. Biochemistry 44 (2005) 11201-11213
    • (2005) Biochemistry , vol.44 , pp. 11201-11213
    • Swint-Kruse, L.1    Zhan, H.2    Matthews, K.S.3
  • 48
    • 33646472260 scopus 로고    scopus 로고
    • Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix
    • Zhan H., Swint-Kruse L., and Matthews K.S. Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix. Biochemistry 45 (2006) 5896-5906
    • (2006) Biochemistry , vol.45 , pp. 5896-5906
    • Zhan, H.1    Swint-Kruse, L.2    Matthews, K.S.3
  • 49
    • 1542350030 scopus 로고    scopus 로고
    • Quantitative analysis and interpretation of allosteric behavior
    • Reinhart G.D. Quantitative analysis and interpretation of allosteric behavior. Methods Enzymol. 380 (2004) 187-203
    • (2004) Methods Enzymol. , vol.380 , pp. 187-203
    • Reinhart, G.D.1
  • 50
    • 0029976830 scopus 로고    scopus 로고
    • Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator
    • Spronk C.A., Slijper M., van Boom J.H., Kaptein R., and Boelens R. Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator. Nat. Struct. Biol. 3 (1996) 916-919
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 916-919
    • Spronk, C.A.1    Slijper, M.2    van Boom, J.H.3    Kaptein, R.4    Boelens, R.5
  • 51
    • 0020381633 scopus 로고
    • Binding of lac repressor induces different conformational changes on operator and non-operator DNAs
    • Culard F., and Maurizot J.C. Binding of lac repressor induces different conformational changes on operator and non-operator DNAs. FEBS Lett. 146 (1982) 153-156
    • (1982) FEBS Lett. , vol.146 , pp. 153-156
    • Culard, F.1    Maurizot, J.C.2
  • 52
    • 4644290827 scopus 로고    scopus 로고
    • Using networks to identify fine structural differences between functionally distinct protein states
    • Swint-Kruse L. Using networks to identify fine structural differences between functionally distinct protein states. Biochemistry 43 (2004) 10886-10895
    • (2004) Biochemistry , vol.43 , pp. 10886-10895
    • Swint-Kruse, L.1
  • 53
    • 0035850794 scopus 로고    scopus 로고
    • Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator
    • Bell C.E., Barry J., Matthews K.S., and Lewis M. Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator. J. Mol. Biol. 313 (2001) 99-109
    • (2001) J. Mol. Biol. , vol.313 , pp. 99-109
    • Bell, C.E.1    Barry, J.2    Matthews, K.S.3    Lewis, M.4
  • 54
    • 0031982791 scopus 로고    scopus 로고
    • Comparison of simulated and experimentally determined dynamics for a variant of the Lacl DNA-binding domain, Nlac-P
    • Swint-Kruse L., Matthews K.S., Smith P.E., and Pettitt B.M. Comparison of simulated and experimentally determined dynamics for a variant of the Lacl DNA-binding domain, Nlac-P. Biophys. J. 74 (1998) 413-421
    • (1998) Biophys. J. , vol.74 , pp. 413-421
    • Swint-Kruse, L.1    Matthews, K.S.2    Smith, P.E.3    Pettitt, B.M.4
  • 55
    • 0036127292 scopus 로고    scopus 로고
    • Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurR
    • Swint-Kruse L., Larson C., Pettitt B.M., and Matthews K.S. Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurR. Protein Sci. 11 (2002) 778-794
    • (2002) Protein Sci. , vol.11 , pp. 778-794
    • Swint-Kruse, L.1    Larson, C.2    Pettitt, B.M.3    Matthews, K.S.4
  • 56
    • 34249891364 scopus 로고    scopus 로고
    • Functional consequences of exchanging domains between LacI and PurR are mediated by the intervening linker sequence
    • Tungtur S., Egan S.M., and Swint-Kruse L. Functional consequences of exchanging domains between LacI and PurR are mediated by the intervening linker sequence. Proteins: Structure, Function, and Bioinformatics 68 (2007) 375-388
    • (2007) Proteins: Structure, Function, and Bioinformatics , vol.68 , pp. 375-388
    • Tungtur, S.1    Egan, S.M.2    Swint-Kruse, L.3
  • 57
    • 0031002095 scopus 로고    scopus 로고
    • Conformation of Lac repressor tetramer in solution, bound and unbound to operator DNA
    • Ruben G.C., and Roos T.B. Conformation of Lac repressor tetramer in solution, bound and unbound to operator DNA. Microsc. Res. Tech. 36 (1997) 400-416
    • (1997) Microsc. Res. Tech. , vol.36 , pp. 400-416
    • Ruben, G.C.1    Roos, T.B.2
  • 59
    • 0037306915 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer over approximately 130 base pairs in hyperstable lac repressor-DNA loops
    • Edelman L.M., Cheong R., and Kahn J.D. Fluorescence resonance energy transfer over approximately 130 base pairs in hyperstable lac repressor-DNA loops. Biophys. J. 84 (2003) 1131-1145
    • (2003) Biophys. J. , vol.84 , pp. 1131-1145
    • Edelman, L.M.1    Cheong, R.2    Kahn, J.D.3
  • 60
    • 19544377327 scopus 로고    scopus 로고
    • Coarse-grained model of entropic allostery
    • Hawkins R.J., and McLeish T.C. Coarse-grained model of entropic allostery. Phys. Rev. Lett. 93 (2004) 098104
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 098104
    • Hawkins, R.J.1    McLeish, T.C.2
  • 61
    • 33745595880 scopus 로고    scopus 로고
    • Modeling the Lac repressor-operator assembly: the influence of DNA looping on Lac repressor conformation
    • Swigon D., Coleman B.D., and Olson W.K. Modeling the Lac repressor-operator assembly: the influence of DNA looping on Lac repressor conformation. Proc. Natl. Acad. Sci. USA 103 (2006) 9879-9884
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9879-9884
    • Swigon, D.1    Coleman, B.D.2    Olson, W.K.3
  • 62
    • 18744391399 scopus 로고    scopus 로고
    • Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation
    • Villa E., Balaeff A., and Schulten K. Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation. Proc. Natl. Acad. Sci. USA 102 (2005) 6783-6788
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6783-6788
    • Villa, E.1    Balaeff, A.2    Schulten, K.3
  • 63
    • 0023660547 scopus 로고
    • Specific destruction of the second lac operator decreases repression of the lac operon in Escherichia coli fivefold
    • Eismann E., von Wilcken-Bergmann B., and Müller-Hill B. Specific destruction of the second lac operator decreases repression of the lac operon in Escherichia coli fivefold. J. Mol. Biol. 195 (1987) 949-952
    • (1987) J. Mol. Biol. , vol.195 , pp. 949-952
    • Eismann, E.1    von Wilcken-Bergmann, B.2    Müller-Hill, B.3
  • 65
  • 66
    • 0018800287 scopus 로고
    • "Second" and "third operator" of the lac operon: an investigation of their role in the regulatory mechanism
    • Pfahl M., Gulde V., and Bourgeois S. "Second" and "third operator" of the lac operon: an investigation of their role in the regulatory mechanism. J. Mol. Biol. 127 (1979) 339-344
    • (1979) J. Mol. Biol. , vol.127 , pp. 339-344
    • Pfahl, M.1    Gulde, V.2    Bourgeois, S.3
  • 67
    • 0022729012 scopus 로고
    • Synthetic lac operator mediates repression through lac repressor when introduced upstream and downstream from lac promoter
    • Besse M., von Wilcken-Bergmann B., and Müller-Hill B. Synthetic lac operator mediates repression through lac repressor when introduced upstream and downstream from lac promoter. EMBO J. 5 (1986) 1377-1381
    • (1986) EMBO J. , vol.5 , pp. 1377-1381
    • Besse, M.1    von Wilcken-Bergmann, B.2    Müller-Hill, B.3
  • 68
    • 0022529619 scopus 로고
    • Upstream operators enhance repression of the lac promoter
    • Mossing M.C., and Record Jr. M.T. Upstream operators enhance repression of the lac promoter. Science 233 (1986) 889-892
    • (1986) Science , vol.233 , pp. 889-892
    • Mossing, M.C.1    Record Jr., M.T.2
  • 69
    • 0025874018 scopus 로고
    • Stability of a Lac repressor mediated "looped complex"
    • Brenowitz M., Pickar A., and Jamison E. Stability of a Lac repressor mediated "looped complex". Biochemistry 30 (1991) 5986-5998
    • (1991) Biochemistry , vol.30 , pp. 5986-5998
    • Brenowitz, M.1    Pickar, A.2    Jamison, E.3
  • 70
    • 0028059578 scopus 로고
    • Subunit dissociation affects DNA binding in a dimeric lac repressor produced by C-terminal deletion
    • Chen J., and Matthews K.S. Subunit dissociation affects DNA binding in a dimeric lac repressor produced by C-terminal deletion. Biochemistry 33 (1994) 8728-8735
    • (1994) Biochemistry , vol.33 , pp. 8728-8735
    • Chen, J.1    Matthews, K.S.2
  • 71
    • 0033987659 scopus 로고    scopus 로고
    • Generation of an Ara-C-araBAD promoter-regulated T7 expression system
    • Wycuff D.R., and Matthews K.S. Generation of an Ara-C-araBAD promoter-regulated T7 expression system. Anal. Biochem. 277 (2000) 67-73
    • (2000) Anal. Biochem. , vol.277 , pp. 67-73
    • Wycuff, D.R.1    Matthews, K.S.2
  • 72
    • 0034641681 scopus 로고    scopus 로고
    • Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein
    • Falcon C.M., and Matthews K.S. Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein. Biochemistry 39 (2000) 11074-11083
    • (2000) Biochemistry , vol.39 , pp. 11074-11083
    • Falcon, C.M.1    Matthews, K.S.2
  • 73
    • 0023055763 scopus 로고
    • Allosteric regulation of inducer and operator binding to the lactose repressor
    • Daly T.J., and Matthews K.S. Allosteric regulation of inducer and operator binding to the lactose repressor. Biochemistry 25 (1986) 5479-5484
    • (1986) Biochemistry , vol.25 , pp. 5479-5484
    • Daly, T.J.1    Matthews, K.S.2
  • 74
    • 0023845141 scopus 로고
    • Comparison of the crystal and solution structures of calmodulin and troponin C
    • Heidorn D.B., and Trewhella J. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry 27 (1988) 909-915
    • (1988) Biochemistry , vol.27 , pp. 909-915
    • Heidorn, D.B.1    Trewhella, J.2
  • 76
    • 0014930863 scopus 로고
    • Molecular con-formation of egg-white lysozyme and bovine alpha-lactalbumin in solution
    • Krigbaum W.R., and Kugler F.R. Molecular con-formation of egg-white lysozyme and bovine alpha-lactalbumin in solution. Biochemistry 9 (1970) 1216-1223
    • (1970) Biochemistry , vol.9 , pp. 1216-1223
    • Krigbaum, W.R.1    Kugler, F.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.