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Volumn 151, Issue 12, 2005, Pages 3979-3987

Dimerization and DNA binding of the Salmonella enterica PhoP response regulator are phosphorylation independent

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BACTERIAL DNA; HISTIDINE; PHOP PROTEIN; TRYPTOPHAN;

EID: 29244483427     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28236-0     Document Type: Article
Times cited : (35)

References (33)
  • 1
    • 0024360445 scopus 로고
    • Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DNA-binding ability
    • Aiba, H., Nakasai, F., Mizushima, S. & Mizuno, T. (1989). Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DNA-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
  • 2
    • 0032739281 scopus 로고    scopus 로고
    • C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli
    • Ames, S. K, Frankema, N. & Kenney, L. J. (1999). C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc Natl Acad Sci U S A 96, 11792-11797.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenney, L.J.3
  • 3
    • 0036174746 scopus 로고    scopus 로고
    • Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
    • Buckler, D. R., Zhou, Y. & Stock, A. M. (2002). Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure 10, 153-164.
    • (2002) Structure , vol.10 , pp. 153-164
    • Buckler, D.R.1    Zhou, Y.2    Stock, A.M.3
  • 4
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in Escherichia coli
    • Cai, S. J. & Inouye, M. (2002). EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J Biol Chem 277, 24155-24161.
    • (2002) J Biol Chem , vol.277 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 6
    • 0034460872 scopus 로고    scopus 로고
    • The unphosphorylated receiver domain of PhoB silences the activity of its output domain
    • Ellison, D. W. & McCleary, W. R. (2000). The unphosphorylated receiver domain of PhoB silences the activity of its output domain. J Bacterial 182, 6592-6597.
    • (2000) J Bacterial , vol.182 , pp. 6592-6597
    • Ellison, D.W.1    McCleary, W.R.2
  • 7
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: Role in resistance to host innate immunity
    • Ernst, R. K, Guina, T. & Miller, S. I. (2001). Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity. Microbes Infect 3, 1327-1334.
    • (2001) Microbes Infect , vol.3 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 8
    • 0029164694 scopus 로고
    • A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules
    • Fiedler, U. & Weiss, V. (1995). A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules. EMBO J 14, 3696-3705.
    • (1995) EMBO J , vol.14 , pp. 3696-3705
    • Fiedler, U.1    Weiss, V.2
  • 9
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84, 165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia-Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 10
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman, E. A. (2001). The pleiotropic two-component regulatory system PhoP-PhoQ. J Bacterial 183, 1835-1842.
    • (2001) J Bacterial , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 11
    • 0343575172 scopus 로고
    • Salmonella typhimurium phoP virulence gene is a transcriptional regulator
    • Groisman, E. A., Chiao, E., Lipps, C. J. & Heffron, F. (1989). Salmonella typhimurium phoP virulence gene is a transcriptional regulator. Proc Natl Acad Sci U S A 86, 7077-7081.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 7077-7081
    • Groisman, E.A.1    Chiao, E.2    Lipps, C.J.3    Heffron, F.4
  • 12
    • 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. (1995). Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J Biol Chem 270, 26849-26856.
    • (1995) J Biol Chem , vol.270 , pp. 26849-26856
    • Harlocker, S.L.1    Bergstrom, L.2    Inouye, M.3
  • 13
    • 0035798619 scopus 로고    scopus 로고
    • Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system
    • Jeon, Y., Lee, Y. S., Han, J. S., Kim, J. B. & Hwang, D. S. (2001). Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system. J Biol Chem 276, 40873-40879.
    • (2001) J Biol Chem , vol.276 , pp. 40873-40879
    • Jeon, Y.1    Lee, Y.S.2    Han, J.S.3    Kim, J.B.4    Hwang, D.S.5
  • 14
    • 0022979404 scopus 로고
    • Purification and characterization of the OmpR protein, a positive regulator involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli
    • Jo, Y. L., Nara, F., Ichihara, S., Mizuno, T. & Mizushima, S. (1986). Purification and characterization of the OmpR protein, a positive regulator involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J Biol Chem 261, 15252-15256.
    • (1986) J Biol Chem , vol.261 , pp. 15252-15256
    • Jo, Y.L.1    Nara, F.2    Ichihara, S.3    Mizuno, T.4    Mizushima, S.5
  • 15
    • 0036214541 scopus 로고    scopus 로고
    • Structure/function relationships in OmpR and other, winged-helix transcription factors
    • Kenney, L. J. (2002). Structure/function relationships in OmpR and other, winged-helix transcription factors. CurrOpinMicrobiol 5, 135-141.
    • (2002) CurrOpinMicrobiol , vol.5 , pp. 135-141
    • Kenney, L.J.1
  • 17
    • 0003320620 scopus 로고    scopus 로고
    • Protein fluorescence
    • 2nd edn, Edited by J. R. Lakowicz. New York: Kluwer Academic/Plenum
    • Lakowicz, J. R. (1999). Protein fluorescence. In Principles of Fluorescence Spectroscopy, 2nd edn, pp. 445-486. Edited by J. R. Lakowicz. New York: Kluwer Academic/Plenum.
    • (1999) Principles of Fluorescence Spectroscopy , pp. 445-486
    • Lakowicz, J.R.1
  • 20
    • 0030809030 scopus 로고    scopus 로고
    • Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter
    • Liu, W. & Hulett, F. M. (1997). Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter. J Bacteriol 179, 6302-6310.
    • (1997) J Bacteriol , vol.179 , pp. 6302-6310
    • Liu, W.1    Hulett, F.M.2
  • 21
    • 0024811077 scopus 로고
    • Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins
    • Makino, K., Shinagawa, H., Amemura, M., Kawamoto, T., Yamada, M. & Nakata, A. (1989). Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J Mol Biol 210, 551-559.
    • (1989) J Mol Biol , vol.210 , pp. 551-559
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kawamoto, T.4    Yamada, M.5    Nakata, A.6
  • 22
    • 0027339446 scopus 로고
    • Role of the σ70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli
    • Makino, K., Amemura, M., Kim, S. K., Nakata, A. & Shinagawa, H. (1993). Role of the σ70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev 7, 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
  • 23
    • 0029896773 scopus 로고    scopus 로고
    • The activation of Pholl by acetylphosphate
    • McCleary, W. R. (1996). The activation of Pholl by acetylphosphate. Mol Microbiol 20, 1155-1163.
    • (1996) Mol Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 25
    • 0035116863 scopus 로고    scopus 로고
    • Characterization of the catalytic activities of the PhoQ histidine protein kinase of Salmonella enterica serovar Typhimurium
    • Montagne, M., Martel, A. & Le Moual, H. (2001). Characterization of the catalytic activities of the PhoQ histidine protein kinase of Salmonella enterica serovar Typhimurium. J Bacteriol 183, 1787-1791.
    • (2001) J Bacteriol , vol.183 , pp. 1787-1791
    • Montagne, M.1    Martel, A.2    Le Moual, H.3
  • 27
    • 0037337511 scopus 로고    scopus 로고
    • Mutational analysis of the residue at position 48 in the Salmonella enterica serovar Typhimurium PhoQ sensor kinase
    • Sanowar, S., Martel, A. & Le Moual, H. (2003). Mutational analysis of the residue at position 48 in the Salmonella enterica serovar Typhimurium PhoQ sensor kinase. J Bacteriol 185, 1935-1941.
    • (2003) J Bacteriol , vol.185 , pp. 1935-1941
    • Sanowar, S.1    Martel, A.2    Le Moual, H.3
  • 28
    • 0025791939 scopus 로고
    • Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the a subunit of RNA polymerase
    • Slauch, J. M., Russo, F. D. & Silhavy, T. J. (1991). Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the a subunit of RNA polymerase. J Bacteriol 173, 7501-7510.
    • (1991) J Bacteriol , vol.173 , pp. 7501-7510
    • Slauch, J.M.1    Russo, F.D.2    Silhavy, T.J.3
  • 29
    • 84902408786 scopus 로고    scopus 로고
    • Response regulator proteins and their interactions with histidine protein kinases
    • Edited by M. Inouye & R. Dutta. New York: Academic Press
    • Stock, A. M. & West, A. H. (2003). Response regulator proteins and their interactions with histidine protein kinases. In Histidine Kinases in Signal Transduction, pp. 237-271. Edited by M. Inouye & R. Dutta. New York: Academic Press.
    • (2003) Histidine Kinases in Signal Transduction , pp. 237-271
    • Stock, A.M.1    West, A.H.2
  • 31
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., Ninfa, A. J. & Stock, A. M. (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
  • 32
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. (1965). The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol 13, 482-495.
    • (1965) J Mol Biol , vol.13 , pp. 482-495
    • Stryer, L.1
  • 33
    • 0036062691 scopus 로고    scopus 로고
    • Novel mode of transcription regulation of divergently overlapping promoters by PhoP, the regulator of two-component system sensing external magnesium availability
    • Yamamoto, K., Ogasawara, H., Fujita, N., Utsumi, R. & Ishihama, A. (2002). Novel mode of transcription regulation of divergently overlapping promoters by PhoP, the regulator of two-component system sensing external magnesium availability. Mol Microbiol 45, 423-438.
    • (2002) Mol Microbiol , vol.45 , pp. 423-438
    • Yamamoto, K.1    Ogasawara, H.2    Fujita, N.3    Utsumi, R.4    Ishihama, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.