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Volumn 326, Issue 1, 2012, Pages 12-22

Signal integration by the Cpx-envelope stress system

Author keywords

Accessory protein; Bacterial cell death; Envelope stress; Inter kingdom signalling; Two component system signalling

Indexed keywords

BACTERIAL PROTEIN; CPXA PROTEIN; CPXP PROTEIN; CPXR PROTEIN; LIPID; METAL; PROTEIN SUBUNIT; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 83055184222     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02436.x     Document Type: Short Survey
Times cited : (96)

References (103)
  • 1
    • 70350057617 scopus 로고    scopus 로고
    • Quality control of cytoplasmic membrane proteins in Escherichia coli
    • Akiyama Y (2009) Quality control of cytoplasmic membrane proteins in Escherichia coli. J Biochem 146: 449-454.
    • (2009) J Biochem , vol.146 , pp. 449-454
    • Akiyama, Y.1
  • 2
    • 78649529371 scopus 로고    scopus 로고
    • Fluidizing the membrane by a local anesthetic: phenylethanol affects membrane protein oligomerization
    • Anbazhagan V, Munz C, Tome L & Schneider D (2010) Fluidizing the membrane by a local anesthetic: phenylethanol affects membrane protein oligomerization. J Mol Biol 404: 773-777.
    • (2010) J Mol Biol , vol.404 , pp. 773-777
    • Anbazhagan, V.1    Munz, C.2    Tome, L.3    Schneider, D.4
  • 3
    • 0042561788 scopus 로고    scopus 로고
    • Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases
    • Appleman JA, Chen L-L & Stewart V (2003) Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases. J Bacteriol 185: 4872-4882.
    • (2003) J Bacteriol , vol.185 , pp. 4872-4882
    • Appleman, J.A.1    Chen, L.-L.2    Stewart, V.3
  • 4
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind L & Ponting CP (1999) The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol Lett 176: 111-116.
    • (1999) FEMS Microbiol Lett , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 6
    • 10744232444 scopus 로고    scopus 로고
    • Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression
    • Beloin C, Valle J, Latour-Lambert P et al. (2004) Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression. Mol Microbiol 51: 659-674.
    • (2004) Mol Microbiol , vol.51 , pp. 659-674
    • Beloin, C.1    Valle, J.2    Latour-Lambert, P.3
  • 7
    • 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 DR & Raivio TL (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
  • 8
    • 75149161574 scopus 로고    scopus 로고
    • Three (and more) component regulatory systems & auxiliary regulators of bacterial histidine kinases
    • Buelow DR & Raivio TL (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
  • 9
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P, Rubio V & Marina A (2009) Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139: 325-336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 10
    • 77949918665 scopus 로고    scopus 로고
    • Sensor domains of two-component regulatory systems
    • Cheung J & Hendrickson WA (2010) Sensor domains of two-component regulatory systems. Curr Opin Microbiol 13: 116-123.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 116-123
    • Cheung, J.1    Hendrickson, W.A.2
  • 11
    • 78751491498 scopus 로고    scopus 로고
    • Characterization of combinatorial patterns generated by multiple two-component sensors in E. coli that respond to many stimuli
    • Clarke EJ & Voigt CA (2011) Characterization of combinatorial patterns generated by multiple two-component sensors in E. coli that respond to many stimuli. Biotechnol Bioeng 108: 666-675.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 666-675
    • Clarke, E.J.1    Voigt, C.A.2
  • 12
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • Dalbey RE, Wang P & Kuhn A (2011) Assembly of bacterial inner membrane proteins. Annu Rev Biochem 80: 161-187.
    • (2011) Annu Rev Biochem , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 13
    • 0030998321 scopus 로고    scopus 로고
    • The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese PN & Silhavy TJ (1997) The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev 11: 1183-1193.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 14
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese PN & Silhavy TJ (1998) CpxP, a stress-combative member of the Cpx regulon. J Bacteriol 180: 831-839.
    • (1998) J Bacteriol , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 15
    • 0031765192 scopus 로고    scopus 로고
    • Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli
    • Danese PN, Oliver GR, Barr K, Bowman GD, Rick PD & Silhavy TJ (1998) Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli. J Bacteriol 180: 5875-5884.
    • (1998) J Bacteriol , vol.180 , pp. 5875-5884
    • Danese, P.N.1    Oliver, G.R.2    Barr, K.3    Bowman, G.D.4    Rick, P.D.5    Silhavy, T.J.6
  • 16
    • 63249116346 scopus 로고    scopus 로고
    • Carbon monoxide-releasing antibacterial molecules target respiration and global transcriptional regulators
    • Davidge KS, Sanguinetti G, Yee CH et al. (2009) Carbon monoxide-releasing antibacterial molecules target respiration and global transcriptional regulators. J Biol Chem 284: 4516-4524.
    • (2009) J Biol Chem , vol.284 , pp. 4516-4524
    • Davidge, K.S.1    Sanguinetti, G.2    Yee, C.H.3
  • 17
    • 0023615466 scopus 로고
    • Mechanism of bactericidal action of aminoglycosides
    • Davis BD (1987) Mechanism of bactericidal action of aminoglycosides. Microbiol Rev 51: 341-350.
    • (1987) Microbiol Rev , vol.51 , pp. 341-350
    • Davis, B.D.1
  • 18
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • DiGiuseppe PA & Silhavy TJ (2003) Signal detection and target gene induction by the CpxRA two-component system. J Bacteriol 185: 2432-2440.
    • (2003) J Bacteriol , vol.185 , pp. 2432-2440
    • DiGiuseppe, P.A.1    Silhavy, T.J.2
  • 19
    • 0021360943 scopus 로고
    • Effects of ethanol on the Escherichia coli plasma membrane
    • Dombek KM & Ingram LO (1984) Effects of ethanol on the Escherichia coli plasma membrane. J Bacteriol 157: 233-239.
    • (1984) J Bacteriol , vol.157 , pp. 233-239
    • Dombek, K.M.1    Ingram, L.O.2
  • 20
    • 0027725286 scopus 로고
    • The deduced amino-acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli
    • Dong JM, Iuchi S, Kwan HS, Lu Z & Lin ECC (1993) The deduced amino-acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. Gene 136: 227-230.
    • (1993) Gene , vol.136 , pp. 227-230
    • Dong, J.M.1    Iuchi, S.2    Kwan, H.S.3    Lu, Z.4    Lin, E.C.C.5
  • 21
    • 0032799155 scopus 로고    scopus 로고
    • Involvement of the Cpx signal transduction pathway of E. coli in biofilm formation
    • Dorel C, Vidal O, Prigent-Combaret C, Vallet I & Lejeune P (1999) Involvement of the Cpx signal transduction pathway of E. coli in biofilm formation. FEMS Microbiol Lett 178: 169-175.
    • (1999) FEMS Microbiol Lett , vol.178 , pp. 169-175
    • Dorel, C.1    Vidal, O.2    Prigent-Combaret, C.3    Vallet, I.4    Lejeune, P.5
  • 22
    • 33646072467 scopus 로고    scopus 로고
    • The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?
    • Dorel C, Lejeune P & Rodrigue A (2006) The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities? Res Microbiol 157: 306-314.
    • (2006) Res Microbiol , vol.157 , pp. 306-314
    • Dorel, C.1    Lejeune, P.2    Rodrigue, A.3
  • 23
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: diversity of domain organization
    • Dutta R, Qin L & Inouye M (1999) Histidine kinases: diversity of domain organization. Mol Microbiol 34: 633-640.
    • (1999) Mol Microbiol , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 24
    • 70349816733 scopus 로고    scopus 로고
    • Role of reactive oxygen species in antibiotic action and resistance
    • Dwyer DJ, Kohanski MA & Collins JJ (2009) Role of reactive oxygen species in antibiotic action and resistance. Curr Opin Microbiol 12: 482-489.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 482-489
    • Dwyer, D.J.1    Kohanski, M.A.2    Collins, J.J.3
  • 25
    • 33646691797 scopus 로고    scopus 로고
    • Global gene expression of a murein (Braun) lipoprotein mutant of Salmonella enterica serovar Typhimurium by microarray analysis
    • Fadl AA, Galindo CL, Sha J, Klimpel GR, Popov VL & Chopra AK (2006) Global gene expression of a murein (Braun) lipoprotein mutant of Salmonella enterica serovar Typhimurium by microarray analysis. Gene 374: 121-127.
    • (2006) Gene , vol.374 , pp. 121-127
    • Fadl, A.A.1    Galindo, C.L.2    Sha, J.3    Klimpel, G.R.4    Popov, V.L.5    Chopra, A.K.6
  • 26
    • 34247880509 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli
    • Fleischer R, Heermann R, Jung K & Hunke S (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
  • 27
    • 33744983969 scopus 로고    scopus 로고
    • Structural classification of bacterial response regulators: diversity of output domains and domain combinations
    • Galperin MY (2006) Structural classification of bacterial response regulators: diversity of output domains and domain combinations. J Bacteriol 188: 4169-4182.
    • (2006) J Bacteriol , vol.188 , pp. 4169-4182
    • Galperin, M.Y.1
  • 28
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin MY, Nikolskaya AN & Koonin EV (2001) Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 203: 11-21.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 29
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao R & Stock AM (2009) Biological insights from structures of two-component proteins. Annu Rev Microbiol 63: 133-154.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 30
    • 0033978494 scopus 로고    scopus 로고
    • Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity
    • Garbe TR, Kobayashi M & Yukawa H (2000) Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity. Arch Microbiol 173: 78-82.
    • (2000) Arch Microbiol , vol.173 , pp. 78-82
    • Garbe, T.R.1    Kobayashi, M.2    Yukawa, H.3
  • 31
    • 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, Leiser OP, Bennion D & Misra R (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
  • 32
    • 0342751307 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34
    • Grass G, Groe C & Nies DH (2000) Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J Bacteriol 182: 1390-1398.
    • (2000) J Bacteriol , vol.182 , pp. 1390-1398
    • Grass, G.1    Groe, C.2    Nies, D.H.3
  • 33
    • 24744452563 scopus 로고    scopus 로고
    • Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations
    • Grass G, Fricke B & Nies DH (2005) Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations. Biometals 18: 437-448.
    • (2005) Biometals , vol.18 , pp. 437-448
    • Grass, G.1    Fricke, B.2    Nies, D.H.3
  • 34
    • 0032568053 scopus 로고    scopus 로고
    • Bacterial chemotaxis: the five sensors of a bacterium
    • Grebe TW & Stock J (1998) Bacterial chemotaxis: the five sensors of a bacterium. Curr Biol 8: R154-R157.
    • (1998) Curr Biol , vol.8
    • Grebe, T.W.1    Stock, J.2
  • 35
    • 67449095110 scopus 로고    scopus 로고
    • Kinetic buffering of cross talk between bacterial two-component sensors
    • Groban ES, Clarke EJ, Salis HM, Miller SM & Voigt CA (2009) Kinetic buffering of cross talk between bacterial two-component sensors. J Mol Biol 390: 380-393.
    • (2009) J Mol Biol , vol.390 , pp. 380-393
    • Groban, E.S.1    Clarke, E.J.2    Salis, H.M.3    Miller, S.M.4    Voigt, C.A.5
  • 36
    • 0029127550 scopus 로고
    • Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli
    • Gupta S, Lee B, Camakaris J & Wu H (1995) Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli. J Bacteriol 177: 4207-4215.
    • (1995) J Bacteriol , vol.177 , pp. 4207-4215
    • Gupta, S.1    Lee, B.2    Camakaris, J.3    Wu, H.4
  • 37
    • 84886972478 scopus 로고    scopus 로고
    • Stimulus perception and signaling in histidine kinases
    • K. Jung & R. Krämer eds) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
    • Heermann R & Jung K (2010) Stimulus perception and signaling in histidine kinases. Bacterial Signaling (K. Jung & R. Krämer eds), pp. 135-161. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
    • (2010) Bacterial Signaling , pp. 135-161
    • Heermann, R.1    Jung, K.2
  • 38
    • 34547661799 scopus 로고    scopus 로고
    • Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli
    • Hirano Y, Hossain MM, Takeda K, Tokuda H & Miki K (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, H.4    Miki, K.5
  • 39
    • 0035794607 scopus 로고    scopus 로고
    • Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili
    • Hung DL, Raivio TL, Jones CH, Silhavy TJ & Hultgren SJ (2001) Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili. EMBO J 20: 1508-1518.
    • (2001) EMBO J , vol.20 , pp. 1508-1518
    • Hung, D.L.1    Raivio, T.L.2    Jones, C.H.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 40
    • 0348147593 scopus 로고    scopus 로고
    • Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli
    • Hunke S & Betton J-M (2003) Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli. Mol Microbiol 50: 1579-1589.
    • (2003) Mol Microbiol , vol.50 , pp. 1579-1589
    • Hunke, S.1    Betton, J.-M.2
  • 41
    • 29144519709 scopus 로고    scopus 로고
    • The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP
    • Isaac DD, Pinkner JS, Hultgren SJ & Silhavy TJ (2005) The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP. P Natl Acad Sci USA 102: 17775-17779.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 17775-17779
    • Isaac, D.D.1    Pinkner, J.S.2    Hultgren, S.J.3    Silhavy, T.J.4
  • 42
    • 0024595996 scopus 로고
    • Differentiation of arcA, arcB, and cpxA mutant phenotypes of Escherichia coli by sex pilus formation and enzyme regulation
    • Iuchi S, Furlong D & Lin EC (1989) Differentiation of arcA, arcB, and cpxA mutant phenotypes of Escherichia coli by sex pilus formation and enzyme regulation. J Bacteriol 171: 2889-2893.
    • (1989) J Bacteriol , vol.171 , pp. 2889-2893
    • Iuchi, S.1    Furlong, D.2    Lin, E.C.3
  • 43
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones CH, Danese PN, Pinkner JS, Silhavy TJ & Hultgren SJ (1997) The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J 16: 6394-6406.
    • (1997) EMBO J , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 44
  • 45
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura H & Beckwith J (2010) Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 13: 1231-1246.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1231-1246
    • Kadokura, H.1    Beckwith, J.2
  • 46
    • 79952280202 scopus 로고    scopus 로고
    • Salmonella Typhi sense host neuroendocrine stress hormones and release the toxin haemolysin E
    • Karavolos MH, Bulmer DM, Spencer H et al. (2011) Salmonella Typhi sense host neuroendocrine stress hormones and release the toxin haemolysin E. EMBO Rep 12: 252-258.
    • (2011) EMBO Rep , vol.12 , pp. 252-258
    • Karavolos, M.H.1    Bulmer, D.M.2    Spencer, H.3
  • 47
    • 69049106304 scopus 로고    scopus 로고
    • Misfolded maltose binding protein MalE219 induces the CpxRA envelope stress response by stimulating phosphoryl transfer from CpxA to CpxR
    • Keller RF & Hunke S (2009) Misfolded maltose binding protein MalE219 induces the CpxRA envelope stress response by stimulating phosphoryl transfer from CpxA to CpxR. Res Microbiol 160: 396-400.
    • (2009) Res Microbiol , vol.160 , pp. 396-400
    • Keller, R.F.1    Hunke, S.2
  • 48
    • 79955154879 scopus 로고    scopus 로고
    • The periplasmic sensor domain of CpxA triggers the CpxA/R phosphorylation cascad
    • Keller R, Havemann J & Hunke S (2011) The periplasmic sensor domain of CpxA triggers the CpxA/R phosphorylation cascad. Res Microbiol 162: 405-409.
    • (2011) Res Microbiol , vol.162 , pp. 405-409
    • Keller, R.1    Havemann, J.2    Hunke, S.3
  • 49
    • 0036214541 scopus 로고    scopus 로고
    • Structure/function relationships in OmpR and other winged-helix transcription factors
    • Kenney LJ (2002) Structure/function relationships in OmpR and other winged-helix transcription factors. Curr Opin Microbiol 5: 135-141.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 135-141
    • Kenney, L.J.1
  • 50
    • 29244442913 scopus 로고    scopus 로고
    • Bacterial histidine kinase as signal sensor and transducer
    • Khorchid A & Ikura M (2006) Bacterial histidine kinase as signal sensor and transducer. Int J Biochem Cell Biol 38: 307-312.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 307-312
    • Khorchid, A.1    Ikura, M.2
  • 51
    • 73649085796 scopus 로고    scopus 로고
    • E Unibus Plurum: genomic analysis of an experimentally evolved polymorphism in Escherichia coli
    • Kinnersley MA, Holben WE & Rosenzweig F (2009) E Unibus Plurum: genomic analysis of an experimentally evolved polymorphism in Escherichia coli. PLoS Genet 5: e1000713.
    • (2009) PLoS Genet , vol.5
    • Kinnersley, M.A.1    Holben, W.E.2    Rosenzweig, F.3
  • 52
    • 34547614468 scopus 로고    scopus 로고
    • The intracellular concentration of acetyl phosphate in Escherichia Coli is sufficient for direct phosphorylation of two-component response regulators
    • Klein AH, Shulla A, Reimann SA, Keating DH & Wolfe AJ (2007) The intracellular concentration of acetyl phosphate in Escherichia Coli is sufficient for direct phosphorylation of two-component response regulators. J Bacteriol 189: 5574-5581.
    • (2007) J Bacteriol , vol.189 , pp. 5574-5581
    • Klein, A.H.1    Shulla, A.2    Reimann, S.A.3    Keating, D.H.4    Wolfe, A.J.5
  • 53
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski MA, Dwyer DJ, Hayete B, Lawrence CA & Collins JJ (2007) A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130: 797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 54
    • 55449126342 scopus 로고    scopus 로고
    • Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death
    • Kohanski MA, Dwyer DJ, Wierzbowski J, Cottarel G & Collins JJ (2008) Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Cell 135: 679-690.
    • (2008) Cell , vol.135 , pp. 679-690
    • Kohanski, M.A.1    Dwyer, D.J.2    Wierzbowski, J.3    Cottarel, G.4    Collins, J.J.5
  • 56
    • 3042610168 scopus 로고    scopus 로고
    • P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli
    • Lee YM, DiGiuseppe PA, Silhavy TJ & Hultgren SJ (2004) P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli. J Bacteriol 186: 4326-4337.
    • (2004) J Bacteriol , vol.186 , pp. 4326-4337
    • Lee, Y.M.1    DiGiuseppe, P.A.2    Silhavy, T.J.3    Hultgren, S.J.4
  • 57
    • 13244271944 scopus 로고    scopus 로고
    • Genome-wide transcriptional response of chemostat-cultured Escherichia Coli to zinc
    • Lee LJ, Barrett JA & Poole RK (2005) Genome-wide transcriptional response of chemostat-cultured Escherichia Coli to zinc. J Bacteriol 187: 1124-1134.
    • (2005) J Bacteriol , vol.187 , pp. 1124-1134
    • Lee, L.J.1    Barrett, J.A.2    Poole, R.K.3
  • 58
    • 80051937249 scopus 로고    scopus 로고
    • Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
    • Lima BP, Antelmann H, Gronau K, Chi BK, Becher D & Wolfe AJ (2011) Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter. Mol Microbiol 81: 1190-1204.
    • (2011) Mol Microbiol , vol.81 , pp. 1190-1204
    • Lima, B.P.1    Antelmann, H.2    Gronau, K.3    Chi, B.K.4    Becher, D.5    Wolfe, A.J.6
  • 59
    • 55949113873 scopus 로고    scopus 로고
    • Two-component signaling and gram negative envelope stress response systems
    • MacRitchie DM, Buelow DR, Price NL & Raivio TL (2008) Two-component signaling and gram negative envelope stress response systems. Adv Exp Med Biol 631: 80-110.
    • (2008) Adv Exp Med Biol , vol.631 , pp. 80-110
    • MacRitchie, D.M.1    Buelow, D.R.2    Price, N.L.3    Raivio, T.L.4
  • 60
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher T, Helmann JD & Unden G (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 70: 910-938.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 61
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • Mileykovskaya E & Dowhan W (1997) The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine. J Bacteriol 179: 1029-1034.
    • (1997) J Bacteriol , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 62
    • 35648955713 scopus 로고    scopus 로고
    • Optimization of the inefficient translation initiation region of the cpxP gene from Escherichia coli
    • Miot M & Betton J-M (2007) Optimization of the inefficient translation initiation region of the cpxP gene from Escherichia coli. Protein Sci 16: 2445-2453.
    • (2007) Protein Sci , vol.16 , pp. 2445-2453
    • Miot, M.1    Betton, J.-M.2
  • 63
    • 0030976053 scopus 로고    scopus 로고
    • Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB
    • Missiakas D & Raina S (1997) Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB. EMBO J 16: 1670-1685.
    • (1997) EMBO J , vol.16 , pp. 1670-1685
    • Missiakas, D.1    Raina, S.2
  • 64
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • Miyadai H, Tanaka-Masuda K, Matsuyama S-I & Tokuda H (2004) Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J Biol Chem 279: 39807-39813.
    • (2004) J Biol Chem , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.-I.3    Tokuda, H.4
  • 65
    • 0030695203 scopus 로고    scopus 로고
    • Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli
    • Mourez M, Skouloubris S, Betton JM & Dassa E (1997) Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli. Mol Microbiol 26: 821-831.
    • (1997) Mol Microbiol , vol.26 , pp. 821-831
    • Mourez, M.1    Skouloubris, S.2    Betton, J.M.3    Dassa, E.4
  • 66
    • 11844292053 scopus 로고    scopus 로고
    • The Cpx envelope stress response affects expression of the Type IV bundle-forming pili of Enteropathogenic Escherichia coli
    • Nevesinjac AZ & Raivio TL (2005) The Cpx envelope stress response affects expression of the Type IV bundle-forming pili of Enteropathogenic Escherichia coli. J Bacteriol 187: 672-686.
    • (2005) J Bacteriol , vol.187 , pp. 672-686
    • Nevesinjac, A.Z.1    Raivio, T.L.2
  • 67
    • 77953948752 scopus 로고    scopus 로고
    • Autoinducer-2 and QseC control biofilm formation and in vivo virulence of Aggregatibacter actinomycetemcomitans
    • Novak EA, Shao H, Daep CA & Demuth DR (2010) Autoinducer-2 and QseC control biofilm formation and in vivo virulence of Aggregatibacter actinomycetemcomitans. Infect Immun 78: 2919-2926.
    • (2010) Infect Immun , vol.78 , pp. 2919-2926
    • Novak, E.A.1    Shao, H.2    Daep, C.A.3    Demuth, D.R.4
  • 68
    • 0037133315 scopus 로고    scopus 로고
    • Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway
    • Otto K & Silhavy TJ (2002) Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway. P Natl Acad Sci USA 99: 2287-2292.
    • (2002) P Natl Acad Sci USA , vol.99 , pp. 2287-2292
    • Otto, K.1    Silhavy, T.J.2
  • 69
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano J, Lynch AS, Belin D, Lin EC & Beckwith J (1997) Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev 11: 1169-1182.
    • (1997) Genes Dev , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.4    Beckwith, J.5
  • 70
    • 0035205423 scopus 로고    scopus 로고
    • Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD Gene
    • Prigent-Combaret C, Brombacher E, Vidal O, Ambert A, Lejeune P, Landini P & Dorel C (2001) Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD Gene. J Bacteriol 183: 7213-7223.
    • (2001) J Bacteriol , vol.183 , pp. 7213-7223
    • Prigent-Combaret, C.1    Brombacher, E.2    Vidal, O.3    Ambert, A.4    Lejeune, P.5    Landini, P.6    Dorel, C.7
  • 71
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • Raffa RG & Raivio TL (2002) A third envelope stress signal transduction pathway in Escherichia coli. Mol Microbiol 45: 1599-1611.
    • (2002) Mol Microbiol , vol.45 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 72
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio TL (2005) Envelope stress responses and Gram-negative bacterial pathogenesis. Mol Microbiol 56: 1119-1128.
    • (2005) Mol Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 73
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio T & Silhavy T (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.1    Silhavy, T.2
  • 74
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • Raivio TL & Silhavy TJ (2001) Periplasmic stress and ECF sigma factors. Annu Rev Microbiol 55: 591-624.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 75
    • 0032851357 scopus 로고    scopus 로고
    • The Cpx envelope stress response is controlled by amplification and feedback inhibition
    • Raivio TL, Popkin DL & Silhavy TJ (1999) The Cpx envelope stress response is controlled by amplification and feedback inhibition. J Bacteriol 181: 5263-5272.
    • (1999) J Bacteriol , vol.181 , pp. 5263-5272
    • Raivio, T.L.1    Popkin, D.L.2    Silhavy, T.J.3
  • 76
    • 0023644949 scopus 로고
    • Conserved domains in bacterial regulatory proteins that respond to environmental stimuli
    • Ronson CW, Nixon BT & Ausubel FM (1987) Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 49: 579-581.
    • (1987) Cell , vol.49 , pp. 579-581
    • Ronson, C.W.1    Nixon, B.T.2    Ausubel, F.M.3
  • 77
    • 33646851752 scopus 로고    scopus 로고
    • Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens
    • Rowley G, Spector M, Kormanec J & Roberts M (2006) Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens. Nat Rev Microbiol 4: 383-394.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 383-394
    • Rowley, G.1    Spector, M.2    Kormanec, J.3    Roberts, M.4
  • 78
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: watchdogs of the Escherichia coli cell envelope
    • Ruiz N & Silhavy TJ (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
  • 80
    • 0035985049 scopus 로고    scopus 로고
    • The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site
    • Shimohata N, Chiba S, Saikawa N, Ito K & Akiyama Y (2002) The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site. Genes Cells 7: 653-662.
    • (2002) Genes Cells , vol.7 , pp. 653-662
    • Shimohata, N.1    Chiba, S.2    Saikawa, N.3    Ito, K.4    Akiyama, Y.5
  • 81
    • 33846571920 scopus 로고    scopus 로고
    • SecY alterations that impair membrane protein folding and generate a membrane stress
    • Shimohata N, Nagamori S, Akiyama Y, Kaback HR & Ito K (2007) SecY alterations that impair membrane protein folding and generate a membrane stress. J Cell Biol 176: 307-317.
    • (2007) J Cell Biol , vol.176 , pp. 307-317
    • Shimohata, N.1    Nagamori, S.2    Akiyama, Y.3    Kaback, H.R.4    Ito, K.5
  • 83
    • 67749135357 scopus 로고    scopus 로고
    • Genetic analysis of activation of the Vibrio cholerae Cpx pathway
    • Slamti L & Waldor MK (2009) Genetic analysis of activation of the Vibrio cholerae Cpx pathway. J Bacteriol 191: 5044-5056.
    • (2009) J Bacteriol , vol.191 , pp. 5044-5056
    • Slamti, L.1    Waldor, M.K.2
  • 84
    • 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, Davis L, Danese P, Cosma C & Silhavy T (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.1    Davis, L.2    Danese, P.3    Cosma, C.4    Silhavy, T.5
  • 85
    • 68449090734 scopus 로고    scopus 로고
    • Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY
    • van Stelten J, Silva F, Belin D & Silhavy TJ (2009) Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY. Science 325: 753-756.
    • (2009) Science , vol.325 , pp. 753-756
    • van Stelten, J.1    Silva, F.2    Belin, D.3    Silhavy, T.J.4
  • 86
    • 75149162101 scopus 로고    scopus 로고
    • The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12
    • Stewart V & Chen L-L (2010) The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12. J Bacteriol 192: 734-745.
    • (2010) J Bacteriol , vol.192 , pp. 734-745
    • Stewart, V.1    Chen, L.-L.2
  • 88
    • 24944591075 scopus 로고    scopus 로고
    • Adenylate cyclase mutations rescue the degP temperature-sensitive phenotype and induce the sigma E and Cpx extracytoplasmic stress regulons in Escherichia coli
    • Strozen TG, Langen GR & Howard SP (2005) Adenylate cyclase mutations rescue the degP temperature-sensitive phenotype and induce the sigma E and Cpx extracytoplasmic stress regulons in Escherichia coli. J Bacteriol 187: 6309-6316.
    • (2005) J Bacteriol , vol.187 , pp. 6309-6316
    • Strozen, T.G.1    Langen, G.R.2    Howard, S.P.3
  • 89
    • 78049387443 scopus 로고    scopus 로고
    • A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system
    • Tao K, Watanabe S, Narita S-I & Tokuda H (2010) A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system. J Bacteriol 192: 5657-5662.
    • (2010) J Bacteriol , vol.192 , pp. 5657-5662
    • Tao, K.1    Watanabe, S.2    Narita, S.-I.3    Tokuda, H.4
  • 90
    • 32244441786 scopus 로고    scopus 로고
    • The DNA-binding domain of the Escherichia coli CpxR two-component response regulator is constitutively active and cannot be fully attenuated by fused adjacent heterologous regulatory domains
    • Tapparel C, Monod A & Kelley WL (2006) The DNA-binding domain of the Escherichia coli CpxR two-component response regulator is constitutively active and cannot be fully attenuated by fused adjacent heterologous regulatory domains. Microbiology 152: 431-441.
    • (2006) Microbiology , vol.152 , pp. 431-441
    • Tapparel, C.1    Monod, A.2    Kelley, W.L.3
  • 92
    • 0034849007 scopus 로고    scopus 로고
    • Role of bundle-forming pilus of enteropathogenic Escherichia coli in host cell adherence and in microcolony development
    • Tobe T & Sasakawa C (2001) Role of bundle-forming pilus of enteropathogenic Escherichia coli in host cell adherence and in microcolony development. Cell Microbiol 3: 579-585.
    • (2001) Cell Microbiol , vol.3 , pp. 579-585
    • Tobe, T.1    Sasakawa, C.2
  • 93
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in Gram-negative bacteria
    • Tokuda H (2009) Biogenesis of outer membranes in Gram-negative bacteria. Biosci Biotechnol Biochem 73: 465-473.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 94
    • 77952802182 scopus 로고    scopus 로고
    • The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus
    • Vogt SL, Nevesinjac AZ, Humphries RM, Donnenberg MS, Armstrong GD & Raivio TL (2010) The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus. Mol Microbiol 76: 1095-1110.
    • (2010) Mol Microbiol , vol.76 , pp. 1095-1110
    • Vogt, S.L.1    Nevesinjac, A.Z.2    Humphries, R.M.3    Donnenberg, M.S.4    Armstrong, G.D.5    Raivio, T.L.6
  • 95
    • 70350211420 scopus 로고    scopus 로고
    • Structural biology of the chaperone-usher pathway of pilus biogenesis
    • Waksman G & Hultgren SJ (2009) Structural biology of the chaperone-usher pathway of pilus biogenesis. Nat Rev Microbiol 7: 765-774.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 765-774
    • Waksman, G.1    Hultgren, S.J.2
  • 96
    • 77950635752 scopus 로고    scopus 로고
    • Global change of gene expression and cell physiology in YidC-depleted Escherichia coli
    • Wang P, Kuhn A & Dalbey RE (2010) Global change of gene expression and cell physiology in YidC-depleted Escherichia coli. J Bacteriol 192: 2193-2209.
    • (2010) J Bacteriol , vol.192 , pp. 2193-2209
    • Wang, P.1    Kuhn, A.2    Dalbey, R.E.3
  • 97
    • 54449093948 scopus 로고    scopus 로고
    • Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA
    • Watanabe S, Oguchi Y, Takeda K, Miki K & Tokuda H (2008) Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA. J Biol Chem 283: 25421-25427.
    • (2008) J Biol Chem , vol.283 , pp. 25421-25427
    • Watanabe, S.1    Oguchi, Y.2    Takeda, K.3    Miki, K.4    Tokuda, H.5
  • 98
    • 0023740169 scopus 로고
    • The Cpx proteins of Escherichia coli K12: structure of the CpxA polypeptide as an inner membrane component
    • Weber RF & Silverman PM (1988) The Cpx proteins of Escherichia coli K12: structure of the CpxA polypeptide as an inner membrane component. J Mol Biol 203: 467-478.
    • (1988) J Mol Biol , vol.203 , pp. 467-478
    • Weber, R.F.1    Silverman, P.M.2
  • 99
    • 41549102957 scopus 로고    scopus 로고
    • Signal Integration by the Two-Component Signal Transduction Response Regulator CpxR
    • Wolfe AJ, Parikh N, Lima BP & Zemaitaitis B (2008) Signal Integration by the Two-Component Signal Transduction Response Regulator CpxR. J Bacteriol 190: 2314-2322.
    • (2008) J Bacteriol , vol.190 , pp. 2314-2322
    • Wolfe, A.J.1    Parikh, N.2    Lima, B.P.3    Zemaitaitis, B.4
  • 100
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto K & Ishihama A (2005) Transcriptional response of Escherichia coli to external copper. Mol Microbiol 56: 215-227.
    • (2005) Mol Microbiol , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 101
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • Yamamoto K & Ishihama A (2006) Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci Biotechnol Biochem 70: 1688-1695.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2
  • 102
    • 43049144591 scopus 로고    scopus 로고
    • The R1 conjugative plasmid increases Escherichia coli biofilm formation through an envelope stress response
    • Yang X, Ma Q & Wood TK (2008) The R1 conjugative plasmid increases Escherichia coli biofilm formation through an envelope stress response. Appl Environ Microbiol 74: 2690-2699.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 2690-2699
    • Yang, X.1    Ma, Q.2    Wood, T.K.3
  • 103
    • 79953229542 scopus 로고    scopus 로고
    • Structural insight into two-component system inhibition and pilus sensing by CpxP
    • Zhou X, Keller R, Volkmer R, Krauß N, Scheerer P & Hunke S (2011) Structural insight into two-component system inhibition and pilus sensing by CpxP. J Biol Chem 286: 9805-9814.
    • (2011) J Biol Chem , vol.286 , pp. 9805-9814
    • Zhou, X.1    Keller, R.2    Volkmer, R.3    Krauß, N.4    Scheerer, P.5    Hunke, S.6


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