메뉴 건너뛰기




Volumn 192, Issue 23, 2010, Pages 6271-6278

MzrA-EnvZ interactions in the periplasm influence the EnvZ/OmpR two-component regulon

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN REGULATOR; PROTEIN ENVZ; PROTEIN MZRA; PROTEIN PHOA; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 78649367258     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00855-10     Document Type: Article
Times cited : (33)

References (39)
  • 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. 264:14090-14094.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14090-14094
    • Aiba, H.1    Nakasai, F.2    Mizushima, S.3    Mizuno, T.4
  • 2
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arié, J.-P., N. Sassoon, and J.-M. Betton. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arié, J.-P.1    Sassoon, N.2    Betton, J.-M.3
  • 3
    • 33845977388 scopus 로고    scopus 로고
    • TorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli
    • Baraquet, C., L. Théraulaz, M. Guiral, D. Lafitte, V. Méjean, and C. Jourlin- Castelli. 2006. TorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli. J. Biol. Chem. 281:38189-38199.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38189-38199
    • Baraquet, C.1    Théraulaz, L.2    Guiral, M.3    Lafitte, D.4    Méjean, V.5    Jourlin-Castelli, C.6
  • 4
    • 33645881935 scopus 로고    scopus 로고
    • Regulation of bacterial virulence by two-component systems
    • Beier, D., and R. Gross. 2006. Regulation of bacterial virulence by two-component systems. Curr. Opin. Microbiol. 9:143-152.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 143-152
    • Beier, D.1    Gross, R.2
  • 5
    • 25144512854 scopus 로고    scopus 로고
    • Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP
    • Buelow, D. R., and T. L. Raivio. 2005. Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP. J. Bacteriol. 187:6622-6630.
    • (2005) J. Bacteriol. , vol.187 , pp. 6622-6630
    • Buelow, D.R.1    Raivio, T.L.2
  • 6
    • 75149161574 scopus 로고    scopus 로고
    • Three (and more) component regulatory systems - Auxiliary regulators of bacterial histidine kinases
    • Buelow, D. R., and T. L. Raivio. 2010. Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases. Mol. Microbiol. 75:547-566.
    • (2010) Mol. Microbiol. , vol.75 , pp. 547-566
    • Buelow, D.R.1    Raivio, T.L.2
  • 7
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M. J. 1976. Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 8
    • 33744993896 scopus 로고    scopus 로고
    • RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli
    • Castanié-Cornet, M.-P., K. Cam, and A. Jacq. 2006. RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli. J. Bacteriol. 188:4264-4270.
    • (2006) J. Bacteriol. , vol.188 , pp. 4264-4270
    • Castanié-Cornet, M.-P.1    Cam, K.2    Jacq, A.3
  • 9
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on the biogenesis of Escherichia coli outer membrane proteins and lipopolysaccharide
    • Charlson, E. S., J. N. Werner, and R. Misra. 2006. Differential effects of yfgL mutation on the biogenesis of Escherichia coli outer membrane proteins and lipopolysaccharide. J. Bacteriol. 188:7186-7194.
    • (2006) J. Bacteriol. , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 12
    • 34247880509 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli
    • Fleischer, R., R. Heermann, K. Jung, and S. Hunke. 2007. Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli. J. Biol. Chem. 282:8583-8593.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8583-8593
    • Fleischer, R.1    Heermann, R.2    Jung, K.3    Hunke, S.4
  • 14
    • 76449101997 scopus 로고    scopus 로고
    • Involvement and necessity of the Cpx regulon in the event of aberrant β-barrel outer membrane protein assembly
    • Gerken, H., O. P. Leiser, D. Bennion, and R. Misra. 2010. Involvement and necessity of the Cpx regulon in the event of aberrant β-barrel outer membrane protein assembly. Mol. Microbiol. 75:1033-1046.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1033-1046
    • Gerken, H.1    Leiser, O.P.2    Bennion, D.3    Misra, R.4
  • 15
    • 33645066654 scopus 로고    scopus 로고
    • Remodeling of the Escherichia coli outer membrane by two small regulatory RNAs
    • Guillier, M., and S. Gottesman. 2006. Remodeling of the Escherichia coli outer membrane by two small regulatory RNAs. Mol. Microbiol. 59:231-247.
    • (2006) Mol. Microbiol. , vol.59 , pp. 231-247
    • Guillier, M.1    Gottesman, S.2
  • 17
    • 34547661799 scopus 로고    scopus 로고
    • Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli
    • Hirano, Y., M. M. Hossain, K. Takeda, T. Tokuda, and K. Miki. 2007. Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli. Structure 15:963-976.
    • (2007) Structure , vol.15 , pp. 963-976
    • Hirano, Y.1    Hossain, M.M.2    Takeda, K.3    Tokuda, T.4    Miki, K.5
  • 19
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ
    • Hsing, W., F. D. Russo, K. K. Bernd, and T. J. Silhavy. 1998. Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J. Bacteriol. 180:4538-4546.
    • (1998) J. Bacteriol. , vol.180 , pp. 4538-4546
    • Hsing, W.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 20
    • 0020059202 scopus 로고
    • Signal sequence of alkaline phosphatase of Escherichia coli
    • Inouye, H., W. Barnes, and J. Beckwith. 1982. Signal sequence of alkaline phosphatase of Escherichia coli. J. Bacteriol. 149:434-439.
    • (1982) J. Bacteriol. , vol.149 , pp. 434-439
    • Inouye, H.1    Barnes, W.2    Beckwith, J.3
  • 22
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., J. Pidoux, A. Ullmann, and D. Ladant. 1998. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U. S. A. 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 24
    • 0027208683 scopus 로고
    • OmpF assembly mutants of Escherichia coli K-12: Isolation, characterization and suppressor analysis
    • Misra, R. 1993. OmpF assembly mutants of Escherichia coli K-12: isolation, characterization and suppressor analysis. J. Bacteriol. 175:5049-5056.
    • (1993) J. Bacteriol. , vol.175 , pp. 5049-5056
    • Misra, R.1
  • 26
    • 0001427734 scopus 로고
    • Porin regulation of Escherichia coli
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, DC
    • Pratt, L. A., and T. J. Silhavy. 1995. Porin regulation of Escherichia coli, p. 105-127. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, DC.
    • (1995) Two-component Signal Transduction , pp. 105-127
    • Pratt, L.A.1    Silhavy, T.J.2
  • 27
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price, N. L., and T. L. Raivio. 2009. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191:1798-1815.
    • (2009) J. Bacteriol. , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 28
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio, T. L., and T. J. Silhavy. 1997. Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J. Bacteriol. 179:7724-7733.
    • (1997) J. Bacteriol. , vol.179 , pp. 7724-7733
    • Raivio, T.L.1    Silhavy, T.J.2
  • 29
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz, N., and T. J. Silhavy. 2005. Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr. Opin. Microbiol. 8:122-126.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 31
    • 0028983261 scopus 로고
    • Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway
    • Snyder, W. B., L. J. B. Davis, P. N. Danese, C. L. Cosma, and T. J. Silhavy. 1995. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J. Bacteriol. 177:4216-4223.
    • (1995) J. Bacteriol. , vol.177 , pp. 4216-4223
    • Snyder, W.B.1    Davis, L.J.B.2    Danese, P.N.3    Cosma, C.L.4    Silhavy, T.J.5
  • 32
    • 0001943573 scopus 로고
    • Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, DC
    • Stewart, V., and R. S. Rabin. 1995. Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli, p. 233-252. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, DC.
    • (1995) Two-component Signal Transduction , pp. 233-252
    • Stewart, V.1    Rabin, R.S.2
  • 33
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K. L., K. Johnson, and J. Beckwith. 1989. Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171:2689-2696.
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 34
    • 0025895382 scopus 로고
    • Transmembrane signal transduction and osmoregulation in Escherichia coli: Functional importance of the periplasmic domain of the membrane-located protein kinase EnvZ
    • Tokishita, S. I., A. Kojima, H. Aiba, and T. Mizuno. 1991. Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the periplasmic domain of the membrane-located protein kinase EnvZ. J. Biol. Chem. 266:6780-6785.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6780-6785
    • Tokishita, S.I.1    Kojima, A.2    Aiba, H.3    Mizuno, T.4
  • 35
    • 0017522339 scopus 로고
    • Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli
    • van Alphen, W., and B. Lugtenberg. 1977. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J. Bacteriol. 131:623-630.
    • (1977) J. Bacteriol. , vol.131 , pp. 623-630
    • Van Alphen, W.1    Lugtenberg, B.2
  • 36
    • 39749086276 scopus 로고    scopus 로고
    • Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
    • DOI 10.1128/JB.01477-07
    • Vuong, P., D. Bennion, J. Mantei, D. Frost, and R. Misra. 2008. Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J. Bacteriol. 190:1507-1517. (Pubitemid 351304004)
    • (2008) Journal of Bacteriology , vol.190 , Issue.5 , pp. 1507-1517
    • Vuong, P.1    Bennion, D.2    Mantei, J.3    Frost, D.4    Misra, R.5
  • 37
    • 23844507131 scopus 로고    scopus 로고
    • YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli
    • Werner, J., and R. Misra. 2005. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 57:1450-1459.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 38
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., J. Malinverni, N. Ruiz, S. Kim, T. J. Silhavy, and D. Kahne. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 39
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • DOI 10.1271/bbb.60024
    • Yamamoto, K., and A. Ishihama. 2006. Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci. Biotechnol. Biochem. 70:1688-1695. (Pubitemid 44124928)
    • (2006) Bioscience, Biotechnology and Biochemistry , vol.70 , Issue.7 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.