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Volumn 290, Issue 1, 1999, Pages 229-240

Domain motions accompanying Tet repressor induction defined by changes of interspin distances at selectively labeled sites

Author keywords

Dipolar interaction; Electron spin resonance spectroscopy; Site directed spin labeling; Spin labels; Tetracycline

Indexed keywords

CYSTEINE; DIMER; NITROXIDE; TETRACYCLINE;

EID: 0033516508     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2875     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0020307662 scopus 로고
    • A multifunctional gene (tetR) controls Tn 10 -encoded tetracycline resistance
    • Beck C. F., Mutzel R., Barbé J., Müller W. A multifunctional gene (tetR) controls Tn 10 -encoded tetracycline resistance. J. Bacteriol. 150:1982;633-642.
    • (1982) J. Bacteriol. , vol.150 , pp. 633-642
    • Beck, C.F.1    Mutzel, R.2    Barbé, J.3    Müller, W.4
  • 2
    • 0031003035 scopus 로고    scopus 로고
    • The role of the variable region in Tet repressor for inducibility by tetracycline
    • Berens C., Schnappinger D., Hillen W. The role of the variable region in Tet repressor for inducibility by tetracycline. J. Biol. Chem. 272:1997;6936-6942.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6936-6942
    • Berens, C.1    Schnappinger, D.2    Hillen, W.3
  • 3
    • 0026489631 scopus 로고
    • Thermal motions of surface α-helices in the D -galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga C. L., Falke J. J. Thermal motions of surface α-helices in the D -galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226:1992;1219-1235.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 4
    • 4043136983 scopus 로고
    • Spin and reaction dynamics in flexible polymethylene biradicals as studied by EPR, NMR, and optical spectroscopy and magnetic field effect. Measurements and mechanisms of scalar electron spin-spin coupling
    • Closs G. L., Forbes M. D. E., Piotrowiak P. Spin and reaction dynamics in flexible polymethylene biradicals as studied by EPR, NMR, and optical spectroscopy and magnetic field effect. Measurements and mechanisms of scalar electron spin-spin coupling. J. Am. Chem. Soc. 114:1992;3285-3294.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3285-3294
    • Closs, G.L.1    Forbes, M.D.E.2    Piotrowiak, P.3
  • 5
    • 0028238102 scopus 로고
    • Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system
    • Cooper A., McAlpine A., Stockley P. G. Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system. FEBS Letters. 348:1994;41-45.
    • (1994) FEBS Letters , vol.348 , pp. 41-45
    • Cooper, A.1    McAlpine, A.2    Stockley, P.G.3
  • 8
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D. L., Altenbach C., Yang K., Hubbell W. L., Khorona H. G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science. 274:1996;768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorona, H.G.5
  • 9
    • 0028989254 scopus 로고
    • Exploring the peptide 3(10)-helix reversible alpha-helix equilibrium with double label electron spin resonance [published erratum appears in Biopolymers (1995) 37, 421]
    • Fiori W. R., Millhauser G. L. Exploring the peptide 3(10)-helix reversible alpha-helix equilibrium with double label electron spin resonance [published erratum appears in Biopolymers (1995) 37, 421]. Biopolymers. 37:1995;243-250.
    • (1995) Biopolymers , vol.37 , pp. 243-250
    • Fiori, W.R.1    Millhauser, G.L.2
  • 10
    • 0002844265 scopus 로고
    • Theory of slow tumbling EPR spectra of nitroxides
    • L. J. Berliner. New York: Academic Press
    • Freed H. Theory of slow tumbling EPR spectra of nitroxides. Berliner L. J. Spin Labeling Theory and Applications. 1976;53-132 Academic Press, New York.
    • (1976) Spin Labeling Theory and Applications , pp. 53-132
    • Freed, H.1
  • 12
    • 0023618036 scopus 로고
    • Engineered Tet repressor mutants with single tryptophan residues as fluorescent probes. Solvent accessibilities of DNA and inducer binding sites and interaction with tetracycline
    • Hansen D., Altschmied L., Hillen W. Engineered Tet repressor mutants with single tryptophan residues as fluorescent probes. Solvent accessibilities of DNA and inducer binding sites and interaction with tetracycline. J. Biol. Chem. 262:1987;14030-14035.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14030-14035
    • Hansen, D.1    Altschmied, L.2    Hillen, W.3
  • 13
    • 0027409473 scopus 로고
    • Noninducible Tet repressor mutations map from the operator binding motif to the C terminus
    • Hecht B., Müller G., Hillen W. Noninducible Tet repressor mutations map from the operator binding motif to the C terminus. J. Bacteriol. 175:1993;1206-1210.
    • (1993) J. Bacteriol. , vol.175 , pp. 1206-1210
    • Hecht, B.1    Müller, G.2    Hillen, W.3
  • 14
    • 0028030082 scopus 로고
    • Mechanisms underlying expression of Tn 10 encoded tetracycline resistance
    • Hillen W., Berens C. Mechanisms underlying expression of Tn 10 encoded tetracycline resistance. Annu. Rev. Microbiol. 48:1994;345-369.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 345-369
    • Hillen, W.1    Berens, C.2
  • 15
    • 0028244325 scopus 로고
    • Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
    • Hinrichs W., Kisker C., Düvel M., Müller A., Tovar K., Hillen W., Saenger W. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science. 264:1994;418-420.
    • (1994) Science , vol.264 , pp. 418-420
    • Hinrichs, W.1    Kisker, C.2    Düvel, M.3    Müller, A.4    Tovar, K.5    Hillen, W.6    Saenger, W.7
  • 16
    • 0028108981 scopus 로고
    • Investigation of structure and dynamics in membrane proteins using site-directed spin labeling
    • Hubbell W. L., Altenbach C. Investigation of structure and dynamics in membrane proteins using site-directed spin labeling. Curr. Opin. Struct. Biol. 4:1994;566-573.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 566-573
    • Hubbell, W.L.1    Altenbach, C.2
  • 19
    • 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
  • 20
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O., Grunert H. P., Hahn U. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene. 96:1990;125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 21
    • 0028924963 scopus 로고
    • Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo
    • Lee G. F., Lebert M. R., Lilly A. A., Hazelbauer G. L. Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo. Proc. Natl Acad. Sci. USA. 92:1995;3391-3395.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3391-3395
    • Lee, G.F.1    Lebert, M.R.2    Lilly, A.A.3    Hazelbauer, G.L.4
  • 23
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • Mchaourab H. S., Oh K. J., Fang C. J., Hubbell W. L. Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry. 36:1997;307-316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • Mchaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 24
  • 25
    • 0029152077 scopus 로고
    • Characterization of non-inducible Tet repressor mutants suggests conformational changes necessary for induction
    • Müller G., Hecht B., Helbl V., Hinrichs W., Saenger W., Hillen W. Characterization of non-inducible Tet repressor mutants suggests conformational changes necessary for induction. Nature Struct. Biol. 2:1995;693-703.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 693-703
    • Müller, G.1    Hecht, B.2    Helbl, V.3    Hinrichs, W.4    Saenger, W.5    Hillen, W.6
  • 26
    • 0032144042 scopus 로고    scopus 로고
    • Structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. Structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8:1998;489-500.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 29
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein M. D., Shin Y. K. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl Acad. Sci. USA. 92:1995;8239-8243.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 31
    • 0029791152 scopus 로고    scopus 로고
    • Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: Application to nitroxide side chains in proteins
    • Steinhoff H.-J., Hubbell W. L. Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: Application to nitroxide side chains in proteins. Biophys. J. 71:1996;2201-2212.
    • (1996) Biophys. J. , vol.71 , pp. 2201-2212
    • Steinhoff, H.-J.1    Hubbell, W.L.2
  • 32
    • 0025718887 scopus 로고
    • Two dimensional diffusions of small molecules on protein surfaces: An EPR study of the restricted translational diffusion of protein bound spin labels
    • Steinhoff H. J., Dombrowsky O., Karim C., Schneiderhan C. Two dimensional diffusions of small molecules on protein surfaces: an EPR study of the restricted translational diffusion of protein bound spin labels. Eur. Biophys. J. 20:1991;293-303.
    • (1991) Eur. Biophys. J. , vol.20 , pp. 293-303
    • Steinhoff, H.J.1    Dombrowsky, O.2    Karim, C.3    Schneiderhan, C.4
  • 35
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the X-ray structure
    • Steinhoff H.-J., Radzwill N., Thevis W., Lenz V., Brandenburg D., Antson A., Dodson G., Wollmer A. Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. Biophys. J. 73:1997;3287-3298.
    • (1997) Biophys. J. , vol.73 , pp. 3287-3298
    • Steinhoff, H.-J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5    Antson, A.6    Dodson, G.7    Wollmer, A.8
  • 36
    • 0022508442 scopus 로고
    • Kinetic and equilibrium characterization of the Tet repressor-tetracycline complex by fluorescence measurements. Evidence for divalent metal ion requirement and energy transfer
    • Takahashi M., Altschmied L., Hillen W. Kinetic and equilibrium characterization of the Tet repressor-tetracycline complex by fluorescence measurements. Evidence for divalent metal ion requirement and energy transfer. J. Mol. Biol. 187:1986;341-348.
    • (1986) J. Mol. Biol. , vol.187 , pp. 341-348
    • Takahashi, M.1    Altschmied, L.2    Hillen, W.3
  • 38
    • 0032167422 scopus 로고    scopus 로고
    • Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation
    • Tiebel B., Aung-Hilbrich L. M., Schnappinger D., Hillen W. Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation. EMBO J. 17:1998;5112-5119.
    • (1998) EMBO J. , vol.17 , pp. 5112-5119
    • Tiebel, B.1    Aung-Hilbrich, L.M.2    Schnappinger, D.3    Hillen, W.4
  • 39
    • 0023256884 scopus 로고
    • The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity
    • Zhang R.-G., Joachimiak A., Lawson C. L., Schevitz R. W., Otwinowski Z., Sigler P. G. The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity. Nature. 327:1987;591-597.
    • (1987) Nature , vol.327 , pp. 591-597
    • Zhang, R.-G.1    Joachimiak, A.2    Lawson, C.L.3    Schevitz, R.W.4    Otwinowski, Z.5    Sigler, P.G.6


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