메뉴 건너뛰기




Volumn 178, Issue 1, 1996, Pages 156-162

The ToxR protein of Vibrio cholerae forms homodimers and heterodimers

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0030059639     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.1.156-162.1996     Document Type: Article
Times cited : (41)

References (33)
  • 1
    • 0024799191 scopus 로고
    • Prokaryotic signal transduction mediated by sensor and regulator protein pairs
    • Albright, L. M., E. Huala, and F. M. Ausubel. 1989. Prokaryotic signal transduction mediated by sensor and regulator protein pairs. Annu. Rev. Genet 23:311-336.
    • (1989) Annu. Rev. Genet , vol.23 , pp. 311-336
    • Albright, L.M.1    Huala, E.2    Ausubel, F.M.3
  • 3
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C. A., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 76:581-589.
    • (1991) Cell , vol.76 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 4
    • 0025803531 scopus 로고
    • The FtsQ protein of Escherichia coli: Membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations
    • Carson, M. J., J. Barondess, and J. Beckwith. 1991. The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. J. Bacteriol. 173:2187-2195
    • (1991) J. Bacteriol. , vol.173 , pp. 2187-2195
    • Carson, M.J.1    Barondess, J.2    Beckwith, J.3
  • 5
    • 0028004066 scopus 로고
    • Altered pH and lysine signaling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon
    • Dell, C. L., M. N. Neely, and E. R. Olson. 1994. Altered pH and lysine signaling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon. Mol. Microbiol. 14:7-16.
    • (1994) Mol. Microbiol. , vol.14 , pp. 7-16
    • Dell, C.L.1    Neely, M.N.2    Olson, E.R.3
  • 6
    • 0026098804 scopus 로고
    • Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation
    • DiRita, V. J., and J. J. Mekalanos. 1991. Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation. Cell 64:29-37.
    • (1991) Cell , vol.64 , pp. 29-37
    • DiRita, V.J.1    Mekalanos, J.J.2
  • 8
    • 0028001591 scopus 로고
    • Analysis of membrane protein interactions: ToxR can dimerize the amino-terminus of lambda repressor
    • Dziejman, M., and J. J. Mekalanos. 1994. Analysis of membrane protein interactions: ToxR can dimerize the amino-terminus of lambda repressor. Mol Microbiol. 13:485-494.
    • (1994) Mol Microbiol. , vol.13 , pp. 485-494
    • Dziejman, M.1    Mekalanos, J.J.2
  • 9
    • 0023224051 scopus 로고
    • Global flexibility in a sensory receptor, a site-directed cross-linking approach
    • Falke, J. J., and D. E. Koshland, Jr. 1987. Global flexibility in a sensory receptor, a site-directed cross-linking approach. Science 237:1596-1600.
    • (1987) Science , vol.237 , pp. 1596-1600
    • Falke, J.J.1    Koshland Jr., D.E.2
  • 10
    • 77956992555 scopus 로고
    • Carboxymethylation
    • Gurd, F. R. N. 1972. Carboxymethylation. Methods Enzymol 25:424-438.
    • (1972) Methods Enzymol , vol.25 , pp. 424-438
    • Gurd, F.R.N.1
  • 11
    • 0028027746 scopus 로고
    • Transcriptional control of toxT, a regulatory gene in the ToxR regulon of Vibrio cholerae
    • Higgins, D. E., and V. J. DiRita. 1994. Transcriptional control of toxT, a regulatory gene in the ToxR regulon of Vibrio cholerae. Mol. Microbiol. 14:17-29.
    • (1994) Mol. Microbiol. , vol.14 , pp. 17-29
    • Higgins, D.E.1    DiRita, V.J.2
  • 12
    • 0026663115 scopus 로고
    • The virulence gene activator ToxT from Vibrio cholerae is a member of the AraC family of transcriptional activators
    • Higgins, D. E., E. Nazareno, and V. J. DiRita. 1992. The virulence gene activator ToxT from Vibrio cholerae is a member of the AraC family of transcriptional activators. J. Bacteriol 174:6874-6980.
    • (1992) J. Bacteriol , vol.174 , pp. 6874-6980
    • Higgins, D.E.1    Nazareno, E.2    DiRita, V.J.3
  • 13
    • 0015714290 scopus 로고
    • Comparison of the tissue receptors for Vibrio cholerae and Escherichia coli enterotoxins by means of gangliosides and natural cholera toxin
    • Holmgren, J. 1973. Comparison of the tissue receptors for Vibrio cholerae and Escherichia coli enterotoxins by means of gangliosides and natural cholera toxin. Infect. Immun 8:851-859.
    • (1973) Infect. Immun , vol.8 , pp. 851-859
    • Holmgren, J.1
  • 14
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar, H., F. Heunecke, K. Götze, B. Junzer, B. Vogt, F. Mayer, and H. Fritz. 1995. Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J 14:3895-3904.
    • (1995) EMBO J , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Heunecke, F.2    Götze, K.3    Junzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.7
  • 16
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis, S., H. Inouye, D. Oliver, and J. Beckwith. 1983 Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J Bactenol. 154:366-374.
    • (1983) J Bactenol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 17
  • 18
    • 0024603180 scopus 로고
    • Identification of toxS. A regulatory gene whose product enhances toxR-mediated activation of the choleia toxin promoter
    • Miller, V. L., V. J. DiRita, and J. J. Mekalanos. 1989. Identification of toxS. a regulatory gene whose product enhances toxR-mediated activation of the choleia toxin promoter J. Bactenol. 171:1288-1293
    • (1989) J. Bactenol. , vol.171 , pp. 1288-1293
    • Miller, V.L.1    DiRita, V.J.2    Mekalanos, J.J.3
  • 19
    • 0542390231 scopus 로고
    • Synthesis of cholera toxin is positively regulated at the transcriptional level by toxR
    • Miller, V. L., and J. J. Mekalanos. 1984. Synthesis of cholera toxin is positively regulated at the transcriptional level by toxR Proc Natl. Acad. Sci. USA 81:3471-3475.
    • (1984) Proc Natl. Acad. Sci. USA , vol.81 , pp. 3471-3475
    • Miller, V.L.1    Mekalanos, J.J.2
  • 20
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations, osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations, osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR J. Bactenol. 170:2575-2583
    • (1988) J. Bactenol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 21
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller, V. L., R. K. Taylor, and J. J. Mekalanos. 1987. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell 48:271-279
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 22
    • 85035158643 scopus 로고    scopus 로고
    • Personal communication
    • Neely, M., and E. Olson. Personal communication.
    • Neely, M.1    Olson, E.2
  • 23
    • 0018828456 scopus 로고
    • Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae
    • Newhall, W. J., W. D. Sawyer, and R. A. Haak. 1980. Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae. Infect. Immun. 28:785-791.
    • (1980) Infect. Immun. , vol.28 , pp. 785-791
    • Newhall, W.J.1    Sawyer, W.D.2    Haak, R.A.3
  • 24
    • 0026715095 scopus 로고
    • ToxR proteins with substitutions in residues conserved with OmpR fail to activate transcription from the cholera toxin promoter
    • Ottemann, K. M., V. J. DiRita, and J. J. Mekalanos. 1992. ToxR proteins with substitutions in residues conserved with OmpR fail to activate transcription from the cholera toxin promoter. J. Bacteriol. 174:6807-6814.
    • (1992) J. Bacteriol. , vol.174 , pp. 6807-6814
    • Ottemann, K.M.1    DiRita, V.J.2    Mekalanos, J.J.3
  • 25
    • 0028951388 scopus 로고
    • Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins
    • Ottemann, K. M., and J. J. Mekalanos. 1995. Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins Mol. Microbiol 15:719-731.
    • (1995) Mol. Microbiol , vol.15 , pp. 719-731
    • Ottemann, K.M.1    Mekalanos, J.J.2
  • 26
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu Rev. Genet. 26:71-112.
    • (1992) Annu Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 28
    • 0017338248 scopus 로고
    • Chemical cross-linking: Reagents and problems in studies of membrane structure
    • Peters, K., and F. M. Richards. 1977. Chemical cross-linking: reagents and problems in studies of membrane structure. Annu. Rev. Biochem. 46:523-551.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 523-551
    • Peters, K.1    Richards, F.M.2
  • 29
    • 0023700080 scopus 로고
    • Characterization of the Vibrio cholerae ToxR regulori: Identification of novel genes involved in intestinal colonization
    • Peterson, K. M., and J. J. Mekalanos. 1988. Characterization of the Vibrio cholerae ToxR regulori: identification of novel genes involved in intestinal colonization. Infect. Immun. 56:2822-2829
    • (1988) Infect. Immun. , vol.56 , pp. 2822-2829
    • Peterson, K.M.1    Mekalanos, J.J.2
  • 31
    • 0020491282 scopus 로고
    • Conformational changes associated with proteolytic processing of presecretory proteins allow glutathione-catalyzed formation of native disulfide bonds
    • Scheele, G., and R. Jacoby. 1982. Conformational changes associated with proteolytic processing of presecretory proteins allow glutathione-catalyzed formation of native disulfide bonds. J. Biol. Chem. 257:12277-12282.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12277-12282
    • Scheele, G.1    Jacoby, R.2
  • 32
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., A. J. Ninfa, and A. M. Stock. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria Microbiol. Rev. 53:450-490.
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 33
    • 0039391898 scopus 로고
    • Use of phoA gene fusions to identify a pilus colonization factor coordinated regulated with cholera toxin
    • Taylor, R. K., V. L. Miller, D. B. Furlong, and J. J. Mekalanos. 1987 Use of phoA gene fusions to identify a pilus colonization factor coordinated regulated with cholera toxin. Proc. Natl. Acad. Sci. USA 84:2833-2837
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2833-2837
    • Taylor, R.K.1    Miller, V.L.2    Furlong, D.B.3    Mekalanos, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.