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Volumn 179, Issue 13, 1997, Pages 4382-4390

Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; HELIX LOOP HELIX PROTEIN; OUTER MEMBRANE PROTEIN; PHOSPHATASE; PHOSPHOTRANSFERASE;

EID: 0030811371     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.13.4382-4390.1997     Document Type: Article
Times cited : (69)

References (45)
  • 1
    • 0024346946 scopus 로고
    • Evidence for the physiological importance of the phosphotransfer between the two regulatory components, EnvZ and OmpR, in osmoregulation in Escherichia coli
    • Aiba, H., F. Nakasai, S. Mizushima, and T. Mizuno. 1989. Evidence for the physiological importance of the phosphotransfer between the two regulatory components, EnvZ and OmpR, in osmoregulation in Escherichia coli. J. Biol. Chem. 269:14090-14094.
    • (1989) J. Biol. Chem. , vol.269 , pp. 14090-14094
    • Aiba, H.1    Nakasai, F.2    Mizushima, S.3    Mizuno, T.4
  • 2
    • 0024338218 scopus 로고
    • Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli
    • Aiba, H., T. Mizuno, and S. Mizushima. 1989. Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J. Biol. Chem. 264:8563-8567.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8563-8567
    • Aiba, H.1    Mizuno, T.2    Mizushima, S.3
  • 3
    • 0024360445 scopus 로고
    • Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DMA-binding ability
    • Aiba, H., F. Nakasai, S. Mizushima, and T. Mizuno. 1989. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DMA-binding ability. J. Biochem. 106:5-7.
    • (1989) J. Biochem. , vol.106 , pp. 5-7
    • Aiba, H.1    Nakasai, F.2    Mizushima, S.3    Mizuno, T.4
  • 4
    • 0024276608 scopus 로고
    • Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output
    • Ames, P., and J. S. Parkinson. 1988. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell 55:817-826.
    • (1988) Cell , vol.55 , pp. 817-826
    • Ames, P.1    Parkinson, J.S.2
  • 5
    • 0028115617 scopus 로고
    • Transmembrane signaling by a hybrid protein: Communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ
    • Baumgartner, J. W., C. H. Kim, R. E. Brissette, M. Inouye, C. K. Park, and G. L. Hazelbauer. 1994. Transmembrane signaling by a hybrid protein: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ. J. Bacteriol. 176:1157-1163.
    • (1994) J. Bacteriol. , vol.176 , pp. 1157-1163
    • Baumgartner, J.W.1    Kim, C.H.2    Brissette, R.E.3    Inouye, M.4    Park, C.K.5    Hazelbauer, G.L.6
  • 6
    • 0026097974 scopus 로고
    • Suppression of a mutation in OmpR at the putative phosphorylation center by a mutant EnvZ protein in Escherichia coli
    • Brissette, R. E., K. Tsung, and M. Inouye. 1991. Suppression of a mutation in OmpR at the putative phosphorylation center by a mutant EnvZ protein in Escherichia coli. J. Bacteriol. 173:601-608.
    • (1991) J. Bacteriol. , vol.173 , pp. 601-608
    • Brissette, R.E.1    Tsung, K.2    Inouye, M.3
  • 7
    • 0026698151 scopus 로고
    • Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
    • Chang, C., and S. C. Winans. 1992. Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein. J. Bacteriol. 174:7033-7039.
    • (1992) J. Bacteriol. , vol.174 , pp. 7033-7039
    • Chang, C.1    Winans, S.C.2
  • 8
    • 0022383830 scopus 로고
    • Primary characterization of the protein products of the Escherichia coli ompB locus: Structure and regulation of synthesis of the OmpR and EnvZ proteins
    • Comeau, D. E., K. Ikenaka, K. Tsung, and M. Inouye. 1985. Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins. J. Bacteriol. 164:578-584.
    • (1985) J. Bacteriol. , vol.164 , pp. 578-584
    • Comeau, D.E.1    Ikenaka, K.2    Tsung, K.3    Inouye, M.4
  • 9
    • 0026006215 scopus 로고
    • Prokaryotic osmoregulation: Genetics and physiology
    • Csonka, L. N., and A. D. Hanson. 1991. Prokaryotic osmoregulation: genetics and physiology. Annu. Rev. Microbiol. 45:569-606.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 569-606
    • Csonka, L.N.1    Hanson, A.D.2
  • 10
    • 0027771353 scopus 로고
    • Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coli
    • Delgado, J., S. Forst, S. Harlocker, and M. Inouye. 1993. Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coli. Mol. Microbiol. 10:1037-1047.
    • (1993) Mol. Microbiol. , vol.10 , pp. 1037-1047
    • Delgado, J.1    Forst, S.2    Harlocker, S.3    Inouye, M.4
  • 11
    • 0030052427 scopus 로고    scopus 로고
    • + mutant of EnvZ EnvZ · N347DJ, a bifunctional signal transducer of Escherichia coli
    • + mutant of EnvZ (EnvZ · N347DJ, a bifunctional signal transducer of Escherichia coli. J. Biol. Chem. 271:1424-1429.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1424-1429
    • Dutta, R.1    Inouye, M.2
  • 12
    • 0024190196 scopus 로고
    • Environmentally regulated gene expression for membrane proteins in Escherichia coli
    • Forst, S., and M. Inouye. 1988. Environmentally regulated gene expression for membrane proteins in Escherichia coli. Annu. Rev. Cell. Biol. 4:21-42.
    • (1988) Annu. Rev. Cell. Biol. , vol.4 , pp. 21-42
    • Forst, S.1    Inouye, M.2
  • 13
    • 0023645956 scopus 로고
    • Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli
    • Forst, S., D. Comeau, S. Norioka, and M. Inouye. 1987. Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli. J. Biol. Chem. 262:16433-16438.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16433-16438
    • Forst, S.1    Comeau, D.2    Norioka, S.3    Inouye, M.4
  • 14
    • 2142806122 scopus 로고
    • Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli
    • Forst, S., J. Delgado, and M. Inouye. 1989. Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli. Proc. Natl. Acad. Sci. USA 86:6052-6056.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6052-6056
    • Forst, S.1    Delgado, J.2    Inouye, M.3
  • 15
    • 0019431325 scopus 로고
    • The ompB locus and the regulation of the major outer membrane porin proteins of Escherichia coli
    • Hall, M. N., and T. J. Silhavy. 1981. The ompB locus and the regulation of the major outer membrane porin proteins of Escherichia coli. J. Mol. Biol. 146:23-43.
    • (1981) J. Mol. Biol. , vol.146 , pp. 23-43
    • Hall, M.N.1    Silhavy, T.J.2
  • 16
    • 0027412041 scopus 로고
    • Phenotypic revertant mutations of a new OmpR2 mutant (V203Q) of Escherichia coli lie in the envZ gene, which encodes the OmpR kinase
    • Harlocker, S. L., A. Rampersaud, W. Yang, and M. Inouye. 1993. Phenotypic revertant mutations of a new OmpR2 mutant (V203Q) of Escherichia coli lie in the envZ gene, which encodes the OmpR kinase. J. Bacteriol. 175:1956-1960.
    • (1993) J. Bacteriol. , vol.175 , pp. 1956-1960
    • Harlocker, S.L.1    Rampersaud, A.2    Yang, W.3    Inouye, M.4
  • 17
    • 0031022042 scopus 로고    scopus 로고
    • Dimer formation of the cytoplasmic domain of a transmembrane osmosensor protein, EnvZ, of Escherichia coli using Ni-histidine tag affinity chromatography
    • Hidaka, Y., H. Park, and M. Inouye. 1996. Dimer formation of the cytoplasmic domain of a transmembrane osmosensor protein, EnvZ, of Escherichia coli using Ni-histidine tag affinity chromatography. FEBS Lett. 400:238-243.
    • (1996) FEBS Lett. , vol.400 , pp. 238-243
    • Hidaka, Y.1    Park, H.2    Inouye, M.3
  • 18
    • 0024759933 scopus 로고
    • Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor
    • Igo, M. M., A. J. Ninfa, J. B. Stock, and T. J. Silhavy. 1989. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3:3725-1734.
    • (1989) Genes Dev. , vol.3 , pp. 3725-11734
    • Igo, M.M.1    Ninfa, A.J.2    Stock, J.B.3    Silhavy, T.J.4
  • 19
    • 0024219910 scopus 로고
    • EnvZ, a transmembrane environmental sensor of Escherichia coli K-12. is phosphorylated in vitro
    • Igo, M. M., and T. J. Silhavy. 1988. EnvZ, a transmembrane environmental sensor of Escherichia coli K-12. is phosphorylated in vitro. J. Bacteriol. 170:5971-5973.
    • (1988) J. Bacteriol. , vol.170 , pp. 5971-5973
    • Igo, M.M.1    Silhavy, T.J.2
  • 20
    • 0025291573 scopus 로고
    • Signal transduction in bacteria: Kinases that control gene expression
    • Igo, M. M., J. M. Slauch, and T. J. Silhavy. 1990. Signal transduction in bacteria: kinases that control gene expression. New Biol. 2:5-9.
    • (1990) New Biol. , vol.2 , pp. 5-9
    • Igo, M.M.1    Slauch, J.M.2    Silhavy, T.J.3
  • 21
    • 0002651060 scopus 로고    scopus 로고
    • His-Asp phosphorelay: Two components or more?
    • Inouye, M. 1996. His-Asp phosphorelay: two components or more? Cell 85:13-14.
    • (1996) Cell , vol.85 , pp. 13-14
    • Inouye, M.1
  • 22
    • 0027202361 scopus 로고
    • Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Tazl
    • Jin, T., and M. Inouye. 1993. Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Tazl. J. Mol. Biol. 232:484-492.
    • (1993) J. Mol. Biol. , vol.232 , pp. 484-492
    • Jin, T.1    Inouye, M.2
  • 23
    • 0025606276 scopus 로고
    • Nitrate- And molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli
    • Kalman, L. V., and R. P. Gunsalus. 1990. Nitrate-and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. J. Bacteriol. 172:7049-7056.
    • (1990) J. Bacteriol. , vol.172 , pp. 7049-7056
    • Kalman, L.V.1    Gunsalus, R.P.2
  • 24
    • 0022921901 scopus 로고
    • Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives
    • Lapilato, J., S. Bortner, and J. Beckwith. 1986. Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives. Mol. Gen. Genet. 205:285-290.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 285-290
    • Lapilato, J.1    Bortner, S.2    Beckwith, J.3
  • 25
    • 0026315513 scopus 로고
    • Three dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M. V., G. G. Prive, D. L. Milligan, W. G. Scott, X. Yen, J. Jancarik, D. E. Koshland, Jr., and S. H. Kim. 1991. Three dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254:1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yen, X.5    Jancarik, J.6    Koshland Jr., D.E.7    Kim, S.H.8
  • 27
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain
    • Monson, E. K., M. Weinstein, G. S. Ditta, and D. R. Helinski. 1992. The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain. Proc. Natl. Acad. Sci. USA 89:4280-4284.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 28
    • 0022571912 scopus 로고
    • Molecular analysis of mutant ompR genes exhibiting different phenotypes as to osmo-regulation of the ompF and ompC genes of Escherichia coli
    • Nara, F., S. Matsuyama, T. Mizuno, and S. Mizushima. 1986. Molecular analysis of mutant ompR genes exhibiting different phenotypes as to osmo-regulation of the ompF and ompC genes of Escherichia coli. Mol. Gen. Genet. 202:194-199.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 194-199
    • Nara, F.1    Matsuyama, S.2    Mizuno, T.3    Mizushima, S.4
  • 29
    • 0027439298 scopus 로고
    • Mechanism of autophosphorylation of Escherichia coli nitrogen regulator II (NRII or NtrB): Trans-phosphorylation between subunits
    • Ninfa, E. G., M. R. Atkinson, E. S. Kamberov, and A. J. Ninfa. 1993. Mechanism of autophosphorylation of Escherichia coli nitrogen regulator II (NRII or NtrB): trans-phosphorylation between subunits. J. Bacteriol. 175: 7024-7032.
    • (1993) J. Bacteriol. , vol.175 , pp. 7024-7032
    • Ninfa, E.G.1    Atkinson, M.R.2    Kamberov, E.S.3    Ninfa, A.J.4
  • 30
    • 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
  • 31
    • 0028289709 scopus 로고
    • Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli
    • Roberts, D. L., D. W. Bennet, and S. A. Forst. 1994. Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. J. Biol. Chem. 269:8728-8733.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8728-8733
    • Roberts, D.L.1    Bennet, D.W.2    Forst, S.A.3
  • 32
    • 0026333013 scopus 로고
    • EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes
    • Russo, F. D., and T. J. Silhavy. 1991. EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes. J. Mol. Biol. 222:567-580.
    • (1991) J. Mol. Biol. , vol.222 , pp. 567-580
    • Russo, F.D.1    Silhavy, T.J.2
  • 33
    • 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
  • 34
    • 0030068603 scopus 로고    scopus 로고
    • Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis
    • Surette, M. G., M. Levit, Y. Liu, G. Lukat, E. G. Ninfa, A. Ninfa, and J. B. Stock. 1996. Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis. J. Biol. Chem. 271:939-945.
    • (1996) J. Biol. Chem. , vol.271 , pp. 939-945
    • Surette, M.G.1    Levit, M.2    Liu, Y.3    Lukat, G.4    Ninfa, E.G.5    Ninfa, A.6    Stock, J.B.7
  • 35
    • 0027156598 scopus 로고
    • Intermolecular complementation of the kinase activity of CheA
    • Swanson, R. V., R. B. Bourret, and M. I. Simon. 1993. Intermolecular complementation of the kinase activity of CheA. Mol. Microbiol. 8:435-441.
    • (1993) Mol. Microbiol. , vol.8 , pp. 435-441
    • Swanson, R.V.1    Bourret, R.B.2    Simon, M.I.3
  • 36
    • 0028030167 scopus 로고
    • Transmembrane signalling by the chimeric chemosensory receptors of Escherichia coli Tsr and Tar with heterologous membrane-spanning regions
    • Tatsuno, I., L. Lee, I. Kawagishi, M. Homma, and Y. Imae. 1994. Transmembrane signalling by the chimeric chemosensory receptors of Escherichia coli Tsr and Tar with heterologous membrane-spanning regions. Mol. Microbiol. 14:755-762.
    • (1994) Mol. Microbiol. , vol.14 , pp. 755-762
    • Tatsuno, I.1    Lee, L.2    Kawagishi, I.3    Homma, M.4    Imae, Y.5
  • 37
    • 0028238973 scopus 로고
    • Mutational activation of CheA, the protein kinase in the chemotaxis system of Escherichia coli
    • Tawa, P., and R. C. Stewart. 1994. Mutational activation of CheA, the protein kinase in the chemotaxis system of Escherichia coli. 5. Bacteriol. 176:4210-4218.
    • (1994) J. Bacteriol. , vol.176 , pp. 4210-4218
    • Tawa, P.1    Stewart, R.C.2
  • 38
    • 0026681093 scopus 로고
    • Transmembrane signal transduction and osmoregulation in Escherichia coli: Functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ
    • Tokishita, S., A. Kojima, and T. Mizuno. 1992. Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ. J. Biochem. 111:707-713.
    • (1992) J. Biochem. , vol.111 , pp. 707-713
    • Tokishita, S.1    Kojima, A.2    Mizuno, T.3
  • 39
    • 0029871035 scopus 로고    scopus 로고
    • Integration of multiple domains in a two-component sensor protein: The Bordetella pertussis BvgAS phosphorelay
    • Uhl, M. A., and J. F. Miller. 1996. Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay. EMBO J. 15:1028-1036.
    • (1996) EMBO J. , vol.15 , pp. 1028-1036
    • Uhl, M.A.1    Miller, J.F.2
  • 40
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi, R., R. E. Brissette, A. Rampersaud, S. A. Forst, K. Oosawa, and M. Inouye. 1989. Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate. Science 245:1246-1249.
    • (1989) Science , vol.245 , pp. 1246-1249
    • Utsumi, R.1    Brissette, R.E.2    Rampersaud, A.3    Forst, S.A.4    Oosawa, K.5    Inouye, M.6
  • 41
    • 0027411096 scopus 로고
    • Gene regulation by phosphate in enteric bacteria
    • Wanner, B. L. 1993. Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 51:47-54.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 47-54
    • Wanner, B.L.1
  • 42
    • 0026603863 scopus 로고
    • Molecular analysis of the signaling pathway betwen EnvZ and OmpR in Escherichta coli
    • Waukau, J., and S. Forst. 1992. Molecular analysis of the signaling pathway betwen EnvZ and OmpR in Escherichta coli. J. Bacteriol. 174:1522-1527.
    • (1992) J. Bacteriol. , vol.174 , pp. 1522-1527
    • Waukau, J.1    Forst, S.2
  • 43
    • 0026322995 scopus 로고
    • Intermolecular complementation between two defective mutant signal transducing receptors of Escherichta coli
    • Yang, Y., and M. Inouye. 1991. Intermolecular complementation between two defective mutant signal transducing receptors of Escherichta coli. Proc. Natl. Acad. Sci. USA 88:11057-11061.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11057-11061
    • Yang, Y.1    Inouye, M.2
  • 44
    • 0027232349 scopus 로고
    • Requirement of both kinase and phosphatase activities of an E. coli: Receptor (Taz1) for figand-dependent signal transduction
    • Yang, Y., and M. Inouye. 1993. Requirement of both kinase and phosphatase activities of an E. coli: receptor (Taz1) for figand-dependent signal transduction. J. Mol. Biol. 231:335-342.
    • (1993) J. Mol. Biol. , vol.231 , pp. 335-342
    • Yang, Y.1    Inouye, M.2
  • 45
    • 0027295668 scopus 로고
    • Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer
    • Yang, Y., H. Park, and M. Inouye. 1993. Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer. J. Mol. Biol. 232; 493-498.
    • (1993) J. Mol. Biol. , vol.232 , pp. 493-498
    • Yang, Y.1    Park, H.2    Inouye, M.3


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