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Volumn 269, Issue 3, 1997, Pages 301-312

Structural relationships in the OmpR family of winged-helix transcription factors

Author keywords

DNA binding protein; Osmoregulation; Response regulator; RNA polymerase; Winged helix turn helix

Indexed keywords

DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; PORIN; REGULATOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0031566431     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1065     Document Type: Review
Times cited : (236)

References (65)
  • 1
    • 0024360445 scopus 로고
    • Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in a stimulation of its DNA-binding ability
    • Aiba H., Nakasai F., Mizushima S., Mizuno T. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in a stimulation of its DNA-binding ability. J. Biochem. 106:1989;5-7.
    • (1989) J. Biochem. , vol.106 , pp. 5-7
    • Aiba, H.1    Nakasai, F.2    Mizushima, S.3    Mizuno, T.4
  • 2
    • 0028094518 scopus 로고
    • Mechanism of gene activation by the Escherichia coli positive regulator, OmpR: A mutant defective in transcriptional activation
    • Aiba H., Kato N., Tsuzuki M., Mizuno T. Mechanism of gene activation by the Escherichia coli positive regulator, OmpR: a mutant defective in transcriptional activation. FEBS Letters. 351:1994;303-307.
    • (1994) FEBS Letters , vol.351 , pp. 303-307
    • Aiba, H.1    Kato, N.2    Tsuzuki, M.3    Mizuno, T.4
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT a tool to format multiple sequence alignments
    • Barton G. J. ALSCRIPT a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 6
    • 0025021988 scopus 로고
    • Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY
    • Bourret R. B., Hess J. F., Simon M. I. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc. Natl Acad. Sci. USA. 87:1990;41-45.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 41-45
    • Bourret, R.B.1    Hess, J.F.2    Simon, M.I.3
  • 7
    • 0027275485 scopus 로고
    • The winged-helix DNA-binding motif: Another helix-turn-helix takeoff
    • Brennan R. G. The winged-helix DNA-binding motif: another helix-turn-helix takeoff. Cell. 74:1993;773-776.
    • (1993) Cell , vol.74 , pp. 773-776
    • Brennan, R.G.1
  • 8
    • 0028061282 scopus 로고
    • Promoter structure, promoter recognition, and transcription activation in prokaryotes
    • Busby S., Ebright R. H. Promoter structure, promoter recognition, and transcription activation in prokaryotes. Cell. 79:1994;743-746.
    • (1994) Cell , vol.79 , pp. 743-746
    • Busby, S.1    Ebright, R.H.2
  • 9
    • 0027423053 scopus 로고
    • Identification, classification, and analysis of beta-bulges in proteins
    • Chan A. W. E., Hutchinson E. G., Harris D., Thornton J. M. Identification, classification, and analysis of beta-bulges in proteins. Protein Sci. 2:1993;1574-1590.
    • (1993) Protein Sci. , vol.2 , pp. 1574-1590
    • Chan, A.W.E.1    Hutchinson, E.G.2    Harris, D.3    Thornton, J.M.4
  • 10
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K. L., Halay E. D., Lai E., Burley S. K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature. 364:1993;412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 11
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12:1984;387-395.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 12
    • 0003084375 scopus 로고
    • Three-component regulatory system controlling virulence in Vibrio cholerae
    • Washington: American Society for Microbiology
    • DiRita V. J. Three-component regulatory system controlling virulence in Vibrio cholerae. Two-component Signal Transduction. 1995;American Society for Microbiology, Washington.
    • (1995) Two-component Signal Transduction
    • Dirita, V.J.1
  • 13
    • 0023185602 scopus 로고
    • Isolation of mutations in the α operon of Escherichia coli that suppress the transcriptional defect conferred by a mutation in the porin regulatory gene envZ
    • Garret S., Silhavy T. J. Isolation of mutations in the α operon of Escherichia coli that suppress the transcriptional defect conferred by a mutation in the porin regulatory gene envZ. J. Bacteriol. 169:1987;1379-1385.
    • (1987) J. Bacteriol. , vol.169 , pp. 1379-1385
    • Garret, S.1    Silhavy, T.J.2
  • 14
    • 0019781275 scopus 로고
    • Genetic analysis of the ompB locus in Escherichia coli K-12
    • Hall M. N., Silhavy T. J. Genetic analysis of the ompB locus in Escherichia coli K-12. J. Mol. Biol. 151:1981;1-15.
    • (1981) J. Mol. Biol. , vol.151 , pp. 1-15
    • Hall, M.N.1    Silhavy, T.J.2
  • 15
    • 0028875660 scopus 로고
    • Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli
    • Harlocker S. L., Bergstrom L., Inouye M. Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J. Biol. Chem. 270:1995;26849-26856.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26849-26856
    • Harlocker, S.L.1    Bergstrom, L.2    Inouye, M.3
  • 16
    • 0030029878 scopus 로고    scopus 로고
    • Genetic analysis of the interaction between Vibrio cholerae transcription activator ToxR and toxT promoter DNA
    • Higgins D. E., DiRita V. J. Genetic analysis of the interaction between Vibrio cholerae transcription activator ToxR and toxT promoter DNA. J. Bacteriol. 178:1996;1080-1087.
    • (1996) J. Bacteriol. , vol.178 , pp. 1080-1087
    • Higgins, D.E.1    Dirita, V.J.2
  • 17
    • 0028204226 scopus 로고
    • Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance inEnterococcus faecium
    • Holman T., Wu Z., Wanner B. L., Walsh C. T. Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance inEnterococcus faecium. Biochemistry. 33:1994;4625-4631.
    • (1994) Biochemistry , vol.33 , pp. 4625-4631
    • Holman, T.1    Wu, Z.2    Wanner, B.L.3    Walsh, C.T.4
  • 18
    • 0030580087 scopus 로고    scopus 로고
    • Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR
    • Huang K. J., Igo M. M. Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR. J. Mol. Biol. 262:1996;615-628.
    • (1996) J. Mol. Biol. , vol.262 , pp. 615-628
    • Huang, K.J.1    Igo, M.M.2
  • 19
    • 0025778597 scopus 로고
    • Bipartite functional map of the E. coli RNA polymerase α subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP
    • Igarashi K., Ishihama A. Bipartite functional map of the E. coli RNA polymerase α subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP. Cell. 65:1991;1015-1022.
    • (1991) Cell , vol.65 , pp. 1015-1022
    • Igarashi, K.1    Ishihama, A.2
  • 20
    • 0025938868 scopus 로고
    • Functional map of the α subunit of Escherichia coli RNA polymerase: Two modes of transcription activation by positive factors
    • Igarashi K., Hanamura A., Makino K., Aiba H., Aiba H., Mizuno T., Nakata T., Ishihama A. Functional map of the α subunit of Escherichia coli RNA polymerase: two modes of transcription activation by positive factors. Proc. Natl Acad. Sci. USA. 88:1991;8958-8962.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8958-8962
    • Igarashi, K.1    Hanamura, A.2    Makino, K.3    Aiba, H.4    Aiba, H.5    Mizuno, T.6    Nakata, T.7    Ishihama, A.8
  • 21
    • 0027262508 scopus 로고
    • Protein-protein communication within the transcription apparatus
    • Ishihama A. Protein-protein communication within the transcription apparatus. J. Bacteriol. 175:1993;2483-2489.
    • (1993) J. Bacteriol. , vol.175 , pp. 2483-2489
    • Ishihama, A.1
  • 22
    • 0029160348 scopus 로고
    • Gene activation by the Escherichia coli positive regulator OmpR: A mutational study of the DNA-binding domain of OmpR
    • Kato N., Tsuzuki M., Aiba H., Mizuno T. Gene activation by the Escherichia coli positive regulator OmpR: a mutational study of the DNA-binding domain of OmpR. Mol. Gen. Genet. 248:1995;399-406.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 399-406
    • Kato, N.1    Tsuzuki, M.2    Aiba, H.3    Mizuno, T.4
  • 23
    • 0029938842 scopus 로고    scopus 로고
    • Suppressor mutations in alpha-subunit of RNA polymerase for a mutant of the positive regulator, OmpR, in Escherichia coli
    • Kato N., Aiba H., Mizuno T. Suppressor mutations in alpha-subunit of RNA polymerase for a mutant of the positive regulator, OmpR, in Escherichia coli. FEMS Microbiol. Letters. 139:1996;175-180.
    • (1996) FEMS Microbiol. Letters , vol.139 , pp. 175-180
    • Kato, N.1    Aiba, H.2    Mizuno, T.3
  • 24
    • 0029026859 scopus 로고
    • Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli
    • Kenney L. J., Bauer M. D., Silhavy T. J. Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli. Proc. Natl Acad. Sci. USA. 92:1995;8866-8870.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8866-8870
    • Kenney, L.J.1    Bauer, M.D.2    Silhavy, T.J.3
  • 26
    • 0031027087 scopus 로고    scopus 로고
    • Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site
    • Kondo H., Nakagawa A., Nishihira J., Nishimura Y., Mizuno T., Tanaka I. Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nature Struct. Biol. 4:1997;28-31.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 28-31
    • Kondo, H.1    Nakagawa, A.2    Nishihira, J.3    Nishimura, Y.4    Mizuno, T.5    Tanaka, I.6
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0027482831 scopus 로고
    • Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: A family of transcription factors of diverse biologic function
    • Lai E., Clark K. L., Burley S. K., Darnell J. E. Jr. Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: A family of transcription factors of diverse biologic function. Proc. Natl Acad. Sci. USA. 90:1993;10421-10423.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10421-10423
    • Lai, E.1    Clark, K.L.2    Burley, S.K.3    Darnell J.E., Jr.4
  • 30
    • 0023801563 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli: Activation of pstS transcription by PhoB protein in vitro
    • Makino K., Shinagawa H., Amemura M., Kimura S., Nakata A., Ishihama A. Regulation of the phosphate regulon of Escherichia coli: activation of pstS transcription by PhoB protein in vitro. J. Mol. Biol. 203:1988;85-95.
    • (1988) J. Mol. Biol. , vol.203 , pp. 85-95
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kimura, S.4    Nakata, A.5    Ishihama, A.6
  • 31
    • 0027339446 scopus 로고
    • Role of the σ70 subunit of RNA polymerase in transcription activation by activator protein PhoB in Escherichia coli
    • Makino K., Amemura M., Kim S.-K., Nakata A., Shinagawa H. Role of the σ70 subunit of RNA polymerase in transcription activation by activator protein PhoB in Escherichia coli. Genes Dev. 7:1993;149-160.
    • (1993) Genes Dev. , vol.7 , pp. 149-160
    • Makino, K.1    Amemura, M.2    Kim, S.-K.3    Nakata, A.4    Shinagawa, H.5
  • 33
    • 0031568318 scopus 로고    scopus 로고
    • The DNA-binding domain of OmpR: Crystal structure of a winged helix transcription factor
    • Martinez-Hackert E., Stock A. M. The DNA-binding domain of OmpR: crystal structure of a winged helix transcription factor. Structure. 5:1997;109-124.
    • (1997) Structure , vol.5 , pp. 109-124
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 34
    • 0023660670 scopus 로고
    • Novel rpoA mutation that interferes with the function of OmpR and EnvZ, positive regulators of theompF and ompC genes that code for the outer-membrane proteins in Escherichia coli K12
    • Matsuyama S., Mizushima S. Novel rpoA mutation that interferes with the function of OmpR and EnvZ, positive regulators of theompF and ompC genes that code for the outer-membrane proteins in Escherichia coli K12. J. Mol. Biol. 195:1987;847-853.
    • (1987) J. Mol. Biol. , vol.195 , pp. 847-853
    • Matsuyama, S.1    Mizushima, S.2
  • 35
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merrit E. A., Murphy M. E. P. Raster3D version 2.0 - A program for photorealistic molecular graphics. Acta Crystallog sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog Sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 36
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller V. L., Taylor R. K., Mekalanos J. J. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell. 48:1987;271-279.
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 37
    • 0028101364 scopus 로고
    • Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae
    • Mills S. D., Lim C. K., Cooksey D. A. Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae. Mol. Gen. Genet. 244:1994;341-351.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 341-351
    • Mills, S.D.1    Lim, C.K.2    Cooksey, D.A.3
  • 38
    • 0023872425 scopus 로고
    • Interaction of OmpR, a positive regulator, with the osmoregulated ompC and ompF genes ofEscherichia coli . Studies with wild-type and mutant OmpR proteins
    • Mizuno T., Kato M., Jo Y., Mizushima S. Interaction of OmpR, a positive regulator, with the osmoregulated ompC and ompF genes ofEscherichia coli . Studies with wild-type and mutant OmpR proteins. J. Biol. Chem. 263:1988;1008-1012.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1008-1012
    • Mizuno, T.1    Kato, M.2    Jo, Y.3    Mizushima, S.4
  • 39
    • 0022993003 scopus 로고
    • Interaction of a transcriptional activator, OmpR, with reciprocally osmoregulated genes, ompF andompC , of Escherichia coli
    • Norioka S., Ramakrishnan G., Ikenaka K., Inouye M. Interaction of a transcriptional activator, OmpR, with reciprocally osmoregulated genes, ompF andompC , of Escherichia coli. J. Biol. Chem. 261:1986;17113-17119.
    • (1986) J. Biol. Chem. , vol.261 , pp. 17113-17119
    • Norioka, S.1    Ramakrishnan, G.2    Ikenaka, K.3    Inouye, M.4
  • 40
    • 0026715095 scopus 로고
    • ToxR proteins with substitutions in residues conserved with OmpR fail to activate transcription from the cholera toxin promoter
    • Ottemann K. M., DiRita V. J., Mekalanos J. J. ToxR proteins with substitutions in residues conserved with OmpR fail to activate transcription from the cholera toxin promoter. J. Bacteriol. 174:1992;6807-6814.
    • (1992) J. Bacteriol. , vol.174 , pp. 6807-6814
    • Ottemann, K.M.1    Dirita, V.J.2    Mekalanos, J.J.3
  • 41
    • 0028103945 scopus 로고
    • Response regulators: Structure, function and evolution
    • Pao G. M., Tam R., Lipschitz L. S., Saier M. H. J. Response regulators: structure, function and evolution. Res. Microbiol. 145:1994;356-362.
    • (1994) Res. Microbiol. , vol.145 , pp. 356-362
    • Pao, G.M.1    Tam, R.2    Lipschitz, L.S.3    Saier, M.H.J.4
  • 42
    • 0030593510 scopus 로고    scopus 로고
    • Structure of the CAP-DNA complex at 2.5 Å resolution: A complete picture of the protein-DNA interface
    • Parkinson G., Wilson C., Gunasekera A., Ebright Y. W., Ebright R. H., Berman H. M. Structure of the CAP-DNA complex at 2.5 Å resolution: a complete picture of the protein-DNA interface. J. Mol. Biol. 260:1996;395-408.
    • (1996) J. Mol. Biol. , vol.260 , pp. 395-408
    • Parkinson, G.1    Wilson, C.2    Gunasekera, A.3    Ebright, Y.W.4    Ebright, R.H.5    Berman, H.M.6
  • 43
    • 0028131766 scopus 로고
    • OmpR mutants specifically defective for transcriptional activation
    • Pratt L. A., Silhavy T. J. OmpR mutants specifically defective for transcriptional activation. J. Mol. Biol. 243:1994;579-594.
    • (1994) J. Mol. Biol. , vol.243 , pp. 579-594
    • Pratt, L.A.1    Silhavy, T.J.2
  • 44
    • 0029157823 scopus 로고
    • Identification of base pairs important for OmpR-DNA interaction
    • Pratt L. A., Silhavy T. J. Identification of base pairs important for OmpR-DNA interaction. Mol. Microbiol. 17:1995a;565-573.
    • (1995) Mol. Microbiol. , vol.17 , pp. 565-573
    • Pratt, L.A.1    Silhavy, T.J.2
  • 45
    • 0001427734 scopus 로고
    • Porin regulon of Escherichia coli
    • J.A. Hoch, & T.J. Silhavy. Washington: American Society for Microbiology
    • Pratt L. A., Silhavy T. J. Porin regulon of Escherichia coli. Hoch J. A., Silhavy T. J. Two-component Signal Transduction. 1995b;American Society for Microbiology, Washington.
    • (1995) Two-component Signal Transduction
    • Pratt, L.A.1    Silhavy, T.J.2
  • 46
    • 0028222516 scopus 로고
    • The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchical manner determined by its degree of phosphorylation
    • Rampersaud A., Harlocker S. L., Inouye M. The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchical manner determined by its degree of phosphorylation. J. Biol. Chem. 269:1994;12559-12566.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12559-12566
    • Rampersaud, A.1    Harlocker, S.L.2    Inouye, M.3
  • 47
    • 0026333013 scopus 로고
    • EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes
    • Russo F., Silhavy T. J. EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes. J. Mol. Biol. 222:1991;567-580.
    • (1991) J. Mol. Biol. , vol.222 , pp. 567-580
    • Russo, F.1    Silhavy, T.J.2
  • 48
    • 0027276137 scopus 로고
    • Mutations that affect separate functions of OmpR the phosphorylated regulator of porin transcription in Escherichia coli
    • Russo F. D., Slauch J. M., Silhavy T. J. Mutations that affect separate functions of OmpR the phosphorylated regulator of porin transcription in Escherichia coli. J. Mol. Biol. 231:1993;261-273.
    • (1993) J. Mol. Biol. , vol.231 , pp. 261-273
    • Russo, F.D.1    Slauch, J.M.2    Silhavy, T.J.3
  • 50
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz S. C., Shields G. C., Steitz T. A. Crystal structure of a CAP-DNA complex: The DNA is bent by 90° Science. 253:1991;1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 51
    • 0027194502 scopus 로고
    • Mutations in the alpha subunit of RNA polymerase that affect the regulation of porin gene transcription inEscherichia coli K-12
    • Sharif T. R., Igo M. M. Mutations in the alpha subunit of RNA polymerase that affect the regulation of porin gene transcription inEscherichia coli K-12. J. Bacteriol. 175:1993;5460-5468.
    • (1993) J. Bacteriol. , vol.175 , pp. 5460-5468
    • Sharif, T.R.1    Igo, M.M.2
  • 52
    • 0024819669 scopus 로고
    • Genetic analysis of the switch that controls porin gene expression in Escherichia coli
    • Slauch J. M., Silhavy T. J. Genetic analysis of the switch that controls porin gene expression in Escherichia coli. J. Mol. Biol. 210:1989;281-292.
    • (1989) J. Mol. Biol. , vol.210 , pp. 281-292
    • Slauch, J.M.1    Silhavy, T.J.2
  • 53
    • 0025739169 scopus 로고
    • Cis -acting ompF mutations that result in OmpR dependent constitutive expression
    • Slauch J. M., Silhavy T. J. cis -acting ompF mutations that result in OmpR dependent constitutive expression. J. Bacteriol. 173:1991;4039-4048.
    • (1991) J. Bacteriol. , vol.173 , pp. 4039-4048
    • Slauch, J.M.1    Silhavy, T.J.2
  • 54
    • 0025791939 scopus 로고
    • Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the alpha subunit of RNA polymerase
    • Slauch J. M., Russo F. D., Silhavy T. J. Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the alpha subunit of RNA polymerase. J. Bacteriol. 173:1991;7501-7510.
    • (1991) J. Bacteriol. , vol.173 , pp. 7501-7510
    • Slauch, J.M.1    Russo, F.D.2    Silhavy, T.J.3
  • 55
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock A. M., Mottonen J. M., Stock J. B., Schutt C. E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature. 337:1989;745-749.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 56
    • 0025271478 scopus 로고
    • Signal transduction in bacteria
    • Stock J. B., Stock A. M., Mottonen J. M. Signal transduction in bacteria. Nature. 344:1990;395-400.
    • (1990) Nature , vol.344 , pp. 395-400
    • Stock, J.B.1    Stock, A.M.2    Mottonen, J.M.3
  • 57
    • 0024213995 scopus 로고
    • Location of DNA-binding segment of a positive regulator, OmpR, involved in activation of the ompF andompC genes of Escherichia coli
    • Tate S., Kato M., Nishimura Y., Arata Y., Mizuno T. Location of DNA-binding segment of a positive regulator, OmpR, involved in activation of the ompF andompC genes of Escherichia coli. FEBS Letters. 242:1988;27-30.
    • (1988) FEBS Letters , vol.242 , pp. 27-30
    • Tate, S.1    Kato, M.2    Nishimura, Y.3    Arata, Y.4    Mizuno, T.5
  • 58
    • 0024382535 scopus 로고
    • Identification of the DNA-binding domain of the OmpR protein required for transcriptional activation of theompF and ompC genes of Escherichia coli by in vivo DNA footprinting
    • Tsung K., Brissette R. E., Inouye M. Identification of the DNA-binding domain of the OmpR protein required for transcriptional activation of theompF and ompC genes of Escherichia coli by in vivo DNA footprinting. J. Biol. Chem. 264:1989;10104-10109.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10104-10109
    • Tsung, K.1    Brissette, R.E.2    Inouye, M.3
  • 59
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution
    • Volz K., Matsumura P. Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution. J. Biol. Chem. 266:1991;15511-15519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 60
    • 0026542813 scopus 로고
    • Identification of elements involved in transcriptional regulation of Escherichia colicad operon by external pH
    • Watson N., Dunyak D. S., Rosey E. L., Slonczewski J. L., Olson E. R. Identification of elements involved in transcriptional regulation of Escherichia colicad operon by external pH. J. Bacteriol. 174:1992;530-540.
    • (1992) J. Bacteriol. , vol.174 , pp. 530-540
    • Watson, N.1    Dunyak, D.S.2    Rosey, E.L.3    Slonczewski, J.L.4    Olson, E.R.5
  • 61
    • 0028785254 scopus 로고
    • The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation
    • Werner M. H., Clore M., Fisher C. L., Fisher R. J., Trinh L., Shiloach J., Gronenborn A. M. The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell. 83:1995;761-771.
    • (1995) Cell , vol.83 , pp. 761-771
    • Werner, M.H.1    Clore, M.2    Fisher, C.L.3    Fisher, R.J.4    Trinh, L.5    Shiloach, J.6    Gronenborn, A.M.7
  • 62
    • 0028854135 scopus 로고
    • Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB
    • West A. H., Martinez-Hackert E., Stock A. M. Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. J. Mol. Biol. 250:1995;276-290.
    • (1995) J. Mol. Biol. , vol.250 , pp. 276-290
    • West, A.H.1    Martinez-Hackert, E.2    Stock, A.M.3
  • 63
    • 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., Matthews B. W. Escherichia 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
  • 64
    • 0025272710 scopus 로고
    • Transcriptional induction of an Agrobacterium regulatory gene at tandem promoters by plant-released phenolic compounds, phosphate starvation, and acidic growth media
    • Winans S. C. Transcriptional induction of an Agrobacterium regulatory gene at tandem promoters by plant-released phenolic compounds, phosphate starvation, and acidic growth media. J. Bacteriol. 172:1990;2433-2438.
    • (1990) J. Bacteriol. , vol.172 , pp. 2433-2438
    • Winans, S.C.1
  • 65
    • 0027161386 scopus 로고
    • Identification of the activating region of catabolyte gene activator protein (CAP): Isolation and characterization of mutants of CAP specifically defective in transcription activation
    • Zhou Y., Zhang X., Ebright R. H. Identification of the activating region of catabolyte gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation. Proc. Natl Acad. Sci. USA. 90:1993;6081-6085.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6081-6085
    • Zhou, Y.1    Zhang, X.2    Ebright, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.