메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 567-575

NMR studies of the Escherichia coli Trp repressor · trpRs operator complex

Author keywords

Deuteration; Trp operator; Trp repressor

Indexed keywords

REPRESSOR PROTEIN; TRYPTOPHAN;

EID: 0030432326     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0567r.x     Document Type: Article
Times cited : (5)

References (38)
  • 1
    • 0026466672 scopus 로고
    • The trp repressor, a ligand activated regulatory protein
    • Somerville, R. L. (1992) The trp repressor, a ligand activated regulatory protein, Prog. Nucleic Acid Res. Mol. Biol 42, 1-38.
    • (1992) Prog. Nucleic Acid Res. Mol. Biol , vol.42 , pp. 1-38
    • Somerville, R.L.1
  • 2
    • 0026525555 scopus 로고
    • Synergism between the Trp repressor and the Tyr repressor in repression of the aroL promoter of Escherichia coli K-12
    • Heatwole, V. M. & Somerville, R. L. (1992) Synergism between the Trp repressor and the Tyr repressor in repression of the aroL promoter of Escherichia coli K-12, J. Bacteriol. 174, 331-335.
    • (1992) J. Bacteriol. , vol.174 , pp. 331-335
    • Heatwole, V.M.1    Somerville, R.L.2
  • 4
    • 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. B. (1987) The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity, Nature 327, 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.B.6
  • 7
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half site complex
    • Lawson, C. L. & Carey, J. (1993) Tandem binding in crystals of a trp repressor/operator half site complex, Nature 366, 178-182.
    • (1993) Nature , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 10
    • 0027528411 scopus 로고
    • Refined solution structures of the Escherichia coli trp holo- And aporepressor
    • Zhao, D., Arrowsmith, C. H., Jia, X. & Jardetzky, O. (1993) Refined solution structures of the Escherichia coli trp holo- and aporepressor, J. Mol. Biol. 229, 735-746.
    • (1993) J. Mol. Biol. , vol.229 , pp. 735-746
    • Zhao, D.1    Arrowsmith, C.H.2    Jia, X.3    Jardetzky, O.4
  • 12
    • 0030022896 scopus 로고    scopus 로고
    • NMR studies of the mode of binding of compressors and inducers to Escherichia coli trp repressor
    • Ramesh, V., Syed, S. E. H., Frederick, R. O., Sutcliffe, M. J., Barnes, M. & Roberts, G. C. K. (1996) NMR studies of the mode of binding of compressors and inducers to Escherichia coli trp repressor, Eur. J. Biochem. 235, 804-813.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 804-813
    • Ramesh, V.1    Syed, S.E.H.2    Frederick, R.O.3    Sutcliffe, M.J.4    Barnes, M.5    Roberts, G.C.K.6
  • 13
    • 0028986817 scopus 로고
    • 15N-labelling of oligonucleotides for NMR: The trp operator and its interactions with the trp repressor
    • 15N-labelling of oligonucleotides for NMR: the trp operator and its interactions with the trp repressor, FEBS Lett. 363, 61-64.
    • (1995) FEBS Lett. , vol.363 , pp. 61-64
    • Ramesh, V.1    Xu, Y.-Z.2    Roberts, G.C.K.3
  • 14
    • 0028283502 scopus 로고
    • A thermodynamic study of the trp repressor-operator interaction
    • Ladbury, J. E., Wright, J. W., Sturtevant, J. M. & Sigler, P. B. (1994) A thermodynamic study of the trp repressor-operator interaction, J. Mol. Biol. 238, 669-681.
    • (1994) J. Mol. Biol. , vol.238 , pp. 669-681
    • Ladbury, J.E.1    Wright, J.W.2    Sturtevant, J.M.3    Sigler, P.B.4
  • 15
    • 0023056195 scopus 로고
    • High level production and rapid purification of the E. coli trp repressor
    • Paluh, J. L. & Yanofsky, C. (1986) High level production and rapid purification of the E. coli trp repressor, Nucleic Acids Res. 14, 7851-7860.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7851-7860
    • Paluh, J.L.1    Yanofsky, C.2
  • 18
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional exchange spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional exchange spectroscopy, J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 19
    • 0019327003 scopus 로고
    • A two dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross relaxation networks in biological molecules
    • Kumar, R. M., Ernst, R. R. & Wüthrich, K. (1980) A two dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross relaxation networks in biological molecules, Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, R.M.1    Ernst, R.R.2    Wüthrich, K.3
  • 20
    • 46549093794 scopus 로고
    • Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy
    • Davis, D. G. & Bax, A. (1985) Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy, J. Magn. Reson. 64, 533-535.
    • (1985) J. Magn. Reson. , vol.64 , pp. 533-535
    • Davis, D.G.1    Bax, A.2
  • 21
    • 5144233105 scopus 로고
    • MLEV-17 based 2D homonuclear magnetisation transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985) MLEV-17 based 2D homonuclear magnetisation transfer spectroscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 22
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing - Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R. R. (1983) Coherence transfer by isotropic mixing - application to proton correlation spectroscopy, J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 24
    • 0026001749 scopus 로고
    • NMR studies of the activation of the Escherichia coli trp repressor
    • Hyde, E. I., Ramesh, V., Frederick, R. & Roberts, G. C. K. (1991) NMR studies of the activation of the Escherichia coli trp repressor, Eur. J. Biochem. 201, 569-579.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 569-579
    • Hyde, E.I.1    Ramesh, V.2    Frederick, R.3    Roberts, G.C.K.4
  • 25
    • 0026042785 scopus 로고
    • Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation
    • Borden, K. L., Beckmann, P. & Lane, A. N. (1991) Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation, Eur. J. Biochem. 202, 459-470.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 459-470
    • Borden, K.L.1    Beckmann, P.2    Lane, A.N.3
  • 26
    • 0028838568 scopus 로고
    • Dynamics of tryptophan binding to the Escherichia coli trp repressor wild type and AV77 mutant: An NMR study
    • Schmitt, T. H., Zheng, Z. & Jardetzky, O. (1995) Dynamics of tryptophan binding to the Escherichia coli trp repressor wild type and AV77 mutant: an NMR study, Biochemistry 34, 13 183-13 189.
    • (1995) Biochemistry , vol.34 , pp. 13183-13189
    • Schmitt, T.H.1    Zheng, Z.2    Jardetzky, O.3
  • 27
    • 0025252231 scopus 로고
    • 1H]-NMR spectroscopy: Combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions
    • 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions, Quart. Rev. Biophys. 23, 39-96.
    • (1990) Quart. Rev. Biophys. , vol.23 , pp. 39-96
    • Otting, G.1    Wüthrich, K.2
  • 28
    • 0000165109 scopus 로고
    • Isotope-filtered 2D NMR of a protein-peptide complex: Studies of a skeletal muscle myosin light chain kinase fragment bound to calmodulin
    • Ikura, M. & Bax, A. (1992) Isotope-filtered 2D NMR of a protein-peptide complex: studies of a skeletal muscle myosin light chain kinase fragment bound to calmodulin, J. Am. Chem. Soc. 114, 2433-2440.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2433-2440
    • Ikura, M.1    Bax, A.2
  • 29
    • 0026834614 scopus 로고
    • The effect of selective deuteration on magnetization transfer in larger proteins
    • Pachter, R., Arrowsmith, C. H. & Jardetzky, O. (1992) The effect of selective deuteration on magnetization transfer in larger proteins, J. Biomol. NMR 2, 183-194.
    • (1992) J. Biomol. NMR , vol.2 , pp. 183-194
    • Pachter, R.1    Arrowsmith, C.H.2    Jardetzky, O.3
  • 30
    • 0024427465 scopus 로고
    • NMR studies of the Escherichia coli trp aporepressor: Sequence specific assignment of the aromatic proton resonances
    • Hyde, E. I., Ramesh, V., Roberts, G. C. K., Arrowsmith, V. H., Treat-Clemons, L., Klaic, B. & Jardetzky, O. (1989) NMR studies of the Escherichia coli trp aporepressor: sequence specific assignment of the aromatic proton resonances, Eur. J. Biochem. 183, 545-553.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 545-553
    • Hyde, E.I.1    Ramesh, V.2    Roberts, G.C.K.3    Arrowsmith, V.H.4    Treat-Clemons, L.5    Klaic, B.6    Jardetzky, O.7
  • 33
    • 0025269342 scopus 로고
    • Deuterium labelling in NMR structural analysis of larger proteins
    • LeMaster, L. E. (1990) Deuterium labelling in NMR structural analysis of larger proteins, Quart. Rev. Biophys. 23, 133- 175.
    • (1990) Quart. Rev. Biophys. , vol.23 , pp. 133-175
    • LeMaster, L.E.1
  • 34
    • 0024284496 scopus 로고
    • Resonance assignments of nonexchangeable protons in B type DNA oligomers, an overview
    • Van de Ven, F. J. M. & Hilbers, C. W. (1988) Resonance assignments of nonexchangeable protons in B type DNA oligomers, an overview, Nucleic Acids Res. 16, 5713-5762.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5713-5762
    • Van De Ven, F.J.M.1    Hilbers, C.W.2
  • 35
    • 0024459036 scopus 로고
    • Tryptophan and 8-anilino-1-napthalene sulphonate compete for binding to trp repressor
    • Chou, W.-Y., Bieber, C. & Matthews, K. S. (1989) Tryptophan and 8-anilino-1-napthalene sulphonate compete for binding to trp repressor, J. Biol. Chem. 264, 18 309-18 313.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18309-18313
    • Chou, W.-Y.1    Bieber, C.2    Matthews, K.S.3
  • 36
    • 0025254056 scopus 로고
    • NMR study of the phosphoryl binding loop in purine nucleotide proteins: Evidence for strong hydrogen bonding in human N-ras p21
    • Redfield, A. G. & Papastavros, M. Z. (1990) NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21, Biochemistry 29, 3509-3514.
    • (1990) Biochemistry , vol.29 , pp. 3509-3514
    • Redfield, A.G.1    Papastavros, M.Z.2
  • 38
    • 0023651152 scopus 로고
    • Solution structure of the trp operator of Escherichia coli determined by NMR
    • Lefevre, J.-F., Lane, A. N. & Jardetzky, O. (1987) Solution structure of the trp operator of Escherichia coli determined by NMR, Biochemistry 26, 5067-5090.
    • (1987) Biochemistry , vol.26 , pp. 5067-5090
    • Lefevre, J.-F.1    Lane, A.N.2    Jardetzky, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.