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Volumn 390, Issue 3, 2009, Pages 380-393

Kinetic Buffering of Cross Talk between Bacterial Two-Component Sensors

Author keywords

computational biology; genetic circuits; synthetic biology; systems biology; two component systems

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN REGULATOR; PROTEIN CPXA; PROTEIN CPXR; PROTEIN ENVZ; UNCLASSIFIED DRUG;

EID: 67449095110     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.05.007     Document Type: Article
Times cited : (78)

References (81)
  • 1
    • 0024042618 scopus 로고
    • Transmitter and receiver modules in bacterial signaling proteins
    • Kofoid E.C., and Parkinson J.S. Transmitter and receiver modules in bacterial signaling proteins. Proc. Natl Acad. Sci. USA 85 (1988) 4981-4985
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4981-4985
    • Kofoid, E.C.1    Parkinson, J.S.2
  • 2
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson J.S., and Kofoid E.C. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26 (1992) 71-112
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 4
    • 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., Mizuno T., and Mizushima S. 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 (1989) 8563-8567
    • (1989) J. Biol. Chem. , vol.264 , pp. 8563-8567
    • Aiba, H.1    Mizuno, T.2    Mizushima, S.3
  • 5
    • 0023644949 scopus 로고
    • Conserved domains in bacterial regulatory proteins that respond to environmental stimuli
    • Ronson C.W., Nixon B.T., and Ausubel F.M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 49 (1987) 579-581
    • (1987) Cell , vol.49 , pp. 579-581
    • Ronson, C.W.1    Nixon, B.T.2    Ausubel, F.M.3
  • 6
    • 0000451424 scopus 로고
    • II, regulates the transcription of the glnALG operon in Escherichia coli
    • II, regulates the transcription of the glnALG operon in Escherichia coli. Proc. Natl Acad. Sci. USA 83 (1986) 5909-5913
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5909-5913
    • Ninfa, A.J.1    Magasanik, B.2
  • 7
    • 0025057053 scopus 로고
    • Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, stimulates the transcription of the ompF and ompC genes in Escherichia coli
    • Aiba H., and Mizuno T. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, stimulates the transcription of the ompF and ompC genes in Escherichia coli. FEBS Lett. 261 (1990) 19-22
    • (1990) FEBS Lett. , vol.261 , pp. 19-22
    • Aiba, H.1    Mizuno, T.2
  • 8
    • 2142806122 scopus 로고
    • Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli
    • Forst S., Delgado J., and Inouye M. Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli. Proc. Natl Acad. Sci. USA 86 (1989) 6052-6056
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6052-6056
    • Forst, S.1    Delgado, J.2    Inouye, M.3
  • 9
    • 0027408328 scopus 로고
    • Bacterial motility and signal transduction
    • Hazelbauer G.L., Berg H.C., and Matsumura P. Bacterial motility and signal transduction. Cell 73 (1993) 15-22
    • (1993) Cell , vol.73 , pp. 15-22
    • Hazelbauer, G.L.1    Berg, H.C.2    Matsumura, P.3
  • 11
    • 0029130181 scopus 로고
    • Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR
    • Shin S., and Park C. Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR. J. Bacteriol. 177 (1995) 4696-4702
    • (1995) J. Bacteriol. , vol.177 , pp. 4696-4702
    • Shin, S.1    Park, C.2
  • 12
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem M., Quadri L.E., Kuipers O.P., and de Vos W.M. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol. Microbiol. 24 (1997) 895-904
    • (1997) Mol. Microbiol. , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.2    Kuipers, O.P.3    de Vos, W.M.4
  • 13
    • 0036844205 scopus 로고    scopus 로고
    • Novel two-component regulatory system involved in biofilm formation and acid resistance in Streptococcus mutans
    • Li Y.H., Lau P.C., Tang N., Svensater G., Ellen R.P., and Cvitkovitch D.G. Novel two-component regulatory system involved in biofilm formation and acid resistance in Streptococcus mutans. J. Bacteriol. 184 (2002) 6333-6342
    • (2002) J. Bacteriol. , vol.184 , pp. 6333-6342
    • Li, Y.H.1    Lau, P.C.2    Tang, N.3    Svensater, G.4    Ellen, R.P.5    Cvitkovitch, D.G.6
  • 14
    • 0141480261 scopus 로고    scopus 로고
    • The roles of SsrA-SsrB and OmpR-EnvZ in the regulation of genes encoding the Salmonella typhimurium SPI-2 type III secretion system
    • Garmendia J., Beuzon C.R., Ruiz-Albert J., and Holden D.W. The roles of SsrA-SsrB and OmpR-EnvZ in the regulation of genes encoding the Salmonella typhimurium SPI-2 type III secretion system. Microbiology 149 (2003) 2385-2396
    • (2003) Microbiology , vol.149 , pp. 2385-2396
    • Garmendia, J.1    Beuzon, C.R.2    Ruiz-Albert, J.3    Holden, D.W.4
  • 15
    • 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., and Lejeune P. Involvement of the Cpx signal transduction pathway of E. coli in biofilm formation. FEMS Microbiol. Lett. 178 (1999) 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
  • 16
    • 0027251261 scopus 로고
    • Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
    • Rabin R.S., and Stewart V. Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12. J. Bacteriol. 175 (1993) 3259-3268
    • (1993) J. Bacteriol. , vol.175 , pp. 3259-3268
    • Rabin, R.S.1    Stewart, V.2
  • 17
    • 0035798620 scopus 로고    scopus 로고
    • + stimulates specifically the autokinase activity of purified and reconstituted EnvZ of Escherichia coli
    • + stimulates specifically the autokinase activity of purified and reconstituted EnvZ of Escherichia coli. J. Biol. Chem. 276 (2001) 40896-40902
    • (2001) J. Biol. Chem. , vol.276 , pp. 40896-40902
    • Jung, K.1    Hamann, K.2    Revermann, A.3
  • 18
    • 0348147587 scopus 로고    scopus 로고
    • The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface
    • Ferrieres L., and Clarke D.J. The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface. Mol. Microbiol. 50 (2003) 1665-1682
    • (2003) Mol. Microbiol. , vol.50 , pp. 1665-1682
    • Ferrieres, L.1    Clarke, D.J.2
  • 19
    • 0028885512 scopus 로고
    • A modified two-component regulatory system is involved in temperature-dependent biosynthesis of the Pseudomonas syringae phytotoxin coronatine
    • Ullrich M., Penaloza-Vazquez A., Bailey A.M., and Bender C.L. A modified two-component regulatory system is involved in temperature-dependent biosynthesis of the Pseudomonas syringae phytotoxin coronatine. J. Bacteriol. 177 (1995) 6160-6169
    • (1995) J. Bacteriol. , vol.177 , pp. 6160-6169
    • Ullrich, M.1    Penaloza-Vazquez, A.2    Bailey, A.M.3    Bender, C.L.4
  • 20
    • 0030865349 scopus 로고    scopus 로고
    • A cyanobacterial phytochrome two-component light sensory system
    • Yeh K.C., Wu S.H., Murphy J.T., and Lagarias J.C. A cyanobacterial phytochrome two-component light sensory system. Science 277 (1997) 1505-1508
    • (1997) Science , vol.277 , pp. 1505-1508
    • Yeh, K.C.1    Wu, S.H.2    Murphy, J.T.3    Lagarias, J.C.4
  • 21
    • 14544286364 scopus 로고    scopus 로고
    • Indole induces the expression of multidrug exporter genes in Escherichia coli
    • Hirakawa H., Inazumi Y., Masaki T., Hirata T., and Yamaguchi A. Indole induces the expression of multidrug exporter genes in Escherichia coli. Mol. Microbiol. 55 (2005) 1113-1126
    • (2005) Mol. Microbiol. , vol.55 , pp. 1113-1126
    • Hirakawa, H.1    Inazumi, Y.2    Masaki, T.3    Hirata, T.4    Yamaguchi, A.5
  • 23
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto K., and Ishihama A. Transcriptional response of Escherichia coli to external copper. Mol. Microbiol. 56 (2005) 215-227
    • (2005) Mol. Microbiol. , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 24
    • 3342908566 scopus 로고    scopus 로고
    • Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis
    • Mascher T., Zimmer S.L., Smith T.A., and Helmann J.D. Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis. Antimicrob. Agents Chemother. 48 (2004) 2888-2896
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2888-2896
    • Mascher, T.1    Zimmer, S.L.2    Smith, T.A.3    Helmann, J.D.4
  • 25
    • 0023731837 scopus 로고
    • Cascade regulation of nif gene expression in Rhizobium meliloti
    • David M., Daveran M.L., Batut J., Dedieu A., Domergue O., Ghai J., et al. Cascade regulation of nif gene expression in Rhizobium meliloti. Cell 54 (1988) 671-683
    • (1988) Cell , vol.54 , pp. 671-683
    • David, M.1    Daveran, M.L.2    Batut, J.3    Dedieu, A.4    Domergue, O.5    Ghai, J.6
  • 26
    • 0032732086 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell division genes ftsA and ftsZ by the two-component system rcsC-rcsB
    • Carballes F., Bertrand C., Bouche J.P., and Cam K. Regulation of Escherichia coli cell division genes ftsA and ftsZ by the two-component system rcsC-rcsB. Mol. Microbiol. 34 (1999) 442-450
    • (1999) Mol. Microbiol. , vol.34 , pp. 442-450
    • Carballes, F.1    Bertrand, C.2    Bouche, J.P.3    Cam, K.4
  • 27
    • 36248980394 scopus 로고    scopus 로고
    • Accurate prediction of gene feedback circuit behavior from component properties
    • Rosenfeld N., Young J.W., Alon U., Swain P.S., and Elowitz M.B. Accurate prediction of gene feedback circuit behavior from component properties. Mol. Syst. Biol. 3 (2007) 143
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 143
    • Rosenfeld, N.1    Young, J.W.2    Alon, U.3    Swain, P.S.4    Elowitz, M.B.5
  • 28
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor C.J., Helman N.C., Yan S., and Lim W.A. Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science 319 (2008) 1539-1543
    • (2008) Science , vol.319 , pp. 1539-1543
    • Bashor, C.J.1    Helman, N.C.2    Yan, S.3    Lim, W.A.4
  • 29
    • 34249885757 scopus 로고    scopus 로고
    • Engineering synthetic signaling proteins with ultrasensitive input/output control
    • Dueber J.E., Mirsky E.A., and Lim W.A. Engineering synthetic signaling proteins with ultrasensitive input/output control. Nat. Biotechnol. 25 (2007) 660-662
    • (2007) Nat. Biotechnol. , vol.25 , pp. 660-662
    • Dueber, J.E.1    Mirsky, E.A.2    Lim, W.A.3
  • 30
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber J.E., Yeh B.J., Chak K., and Lim W.A. Reprogramming control of an allosteric signaling switch through modular recombination. Science 301 (2003) 1904-1908
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 31
    • 0036174746 scopus 로고    scopus 로고
    • Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
    • Buckler D.R., Zhou Y., and Stock A.M. Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure 10 (2002) 153-164
    • (2002) Structure , vol.10 , pp. 153-164
    • Buckler, D.R.1    Zhou, Y.2    Stock, A.M.3
  • 33
    • 0344142378 scopus 로고    scopus 로고
    • Three-dimensional crystal structure of the transcription factor PhoB receiver domain
    • Sola M., Gomis-Ruth F.X., Serrano L., Gonzalez A., and Coll M. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J. Mol. Biol. 285 (1999) 675-687
    • (1999) J. Mol. Biol. , vol.285 , pp. 675-687
    • Sola, M.1    Gomis-Ruth, F.X.2    Serrano, L.3    Gonzalez, A.4    Coll, M.5
  • 34
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution
    • Volz K., and Matsumura P. Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution. J. Biol. Chem. 266 (1991) 15511-15519
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 35
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi R., Brissette R.E., Rampersaud A., Forst S.A., Oosawa K., and Inouye M. Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate. Science 245 (1989) 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
  • 36
    • 0028115617 scopus 로고
    • Transmembrane signalling 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., Kim C., Brissette R.E., Inouye M., Park C., and Hazelbauer G.L. Transmembrane signalling 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 (1994) 1157-1163
    • (1994) J. Bacteriol. , vol.176 , pp. 1157-1163
    • Baumgartner, J.W.1    Kim, C.2    Brissette, R.E.3    Inouye, M.4    Park, C.5    Hazelbauer, G.L.6
  • 37
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger L.L., Dwyer M.A., Smith J.J., and Hellinga H.W. Computational design of receptor and sensor proteins with novel functions. Nature 423 (2003) 185-190
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 39
    • 0036091152 scopus 로고    scopus 로고
    • A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite
    • Ward S.M., Delgado A., Gunsalus R.P., and Manson M.D. A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite. Mol. Microbiol. 44 (2002) 709-719
    • (2002) Mol. Microbiol. , vol.44 , pp. 709-719
    • Ward, S.M.1    Delgado, A.2    Gunsalus, R.P.3    Manson, M.D.4
  • 41
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub M.T., and Goulian M. Specificity in two-component signal transduction pathways. Annu. Rev. Genet. 41 (2007) 121-145
    • (2007) Annu. Rev. Genet. , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 43
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock J.B., Ninfa A.J., and Stock A.M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53 (1989) 450-490
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 44
    • 16244402636 scopus 로고    scopus 로고
    • Bacterial observations: a rudimentary form of intelligence?
    • Hellingwerf K.J. Bacterial observations: a rudimentary form of intelligence?. Trends Microbiol. 13 (2005) 152-158
    • (2005) Trends Microbiol. , vol.13 , pp. 152-158
    • Hellingwerf, K.J.1
  • 46
    • 0037383238 scopus 로고    scopus 로고
    • Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: differences in molecular structure and physiological function
    • Alves R., and Savageau M.A. Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: differences in molecular structure and physiological function. Mol. Microbiol. 48 (2003) 25-51
    • (2003) Mol. Microbiol. , vol.48 , pp. 25-51
    • Alves, R.1    Savageau, M.A.2
  • 47
    • 52649164147 scopus 로고    scopus 로고
    • Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli
    • Siryaporn A., and Goulian M. Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli. Mol. Microbiol. 70 (2008) 494-506
    • (2008) Mol. Microbiol. , vol.70 , pp. 494-506
    • Siryaporn, A.1    Goulian, M.2
  • 48
    • 0032477825 scopus 로고    scopus 로고
    • Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis
    • Grimshaw C.E., Huang S., Hanstein C.G., Strauch M.A., Burbulys D., Wang L., et al. Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis. Biochemistry 37 (1998) 1365-1375
    • (1998) Biochemistry , vol.37 , pp. 1365-1375
    • Grimshaw, C.E.1    Huang, S.2    Hanstein, C.G.3    Strauch, M.A.4    Burbulys, D.5    Wang, L.6
  • 49
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., and Ishihama A. Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J. Biol. Chem. 280 (2005) 1448-1456
    • (2005) J. Biol. Chem. , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 50
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis
    • Skerker J.M., Prasol M.S., Perchuk B.S., Biondi E.G., and Laub M.T. Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol. 3 (2005) e334
    • (2005) PLoS Biol. , vol.3
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 51
    • 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 J., Iuchi S., Kwan H.S., Lu Z., and Lin E.C. 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 (1993) 227-230
    • (1993) Gene , vol.136 , pp. 227-230
    • Dong, J.1    Iuchi, S.2    Kwan, H.S.3    Lu, Z.4    Lin, E.C.5
  • 52
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • De Wulf P., McGuire A.M., Liu X., and Lin E.C. Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli. J. Biol. Chem. 277 (2002) 26652-26661
    • (2002) J. Biol. Chem. , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 53
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio T.L. Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56 (2005) 1119-1128
    • (2005) Mol. Microbiol. , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 54
    • 23644456999 scopus 로고    scopus 로고
    • The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins ompF and ompC
    • Batchelor E., Walthers D., Kenney L.J., and Goulian M. The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins ompF and ompC. J. Bacteriol. 187 (2005) 5723-5731
    • (2005) J. Bacteriol. , vol.187 , pp. 5723-5731
    • Batchelor, E.1    Walthers, D.2    Kenney, L.J.3    Goulian, M.4
  • 56
    • 0024759933 scopus 로고
    • Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor
    • Igo M.M., Ninfa A.J., Stock J.B., and Silhavy T.J. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3 (1989) 1725-1734
    • (1989) Genes Dev. , vol.3 , pp. 1725-1734
    • Igo, M.M.1    Ninfa, A.J.2    Stock, J.B.3    Silhavy, T.J.4
  • 57
    • 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, Taz1
    • Jin T., and Inouye M. 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, Taz1. J. Mol. Biol. 232 (1993) 484-492
    • (1993) J. Mol. Biol. , vol.232 , pp. 484-492
    • Jin, T.1    Inouye, M.2
  • 58
    • 0024061466 scopus 로고
    • Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism
    • Ninfa A.J., Ninfa E.G., Lupas A.N., Stock A., Magasanik B., and Stock J. Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proc. Natl Acad. Sci. USA 85 (1988) 5492-5496
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 5492-5496
    • Ninfa, A.J.1    Ninfa, E.G.2    Lupas, A.N.3    Stock, A.4    Magasanik, B.5    Stock, J.6
  • 59
    • 0033962665 scopus 로고    scopus 로고
    • Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes
    • De Wulf P., and Lin E.C. Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes. J. Bacteriol. 182 (2000) 1423-1426
    • (2000) J. Bacteriol. , vol.182 , pp. 1423-1426
    • De Wulf, P.1    Lin, E.C.2
  • 60
    • 41549102957 scopus 로고    scopus 로고
    • Signal integration by the two-component signal transduction response regulator CpxR
    • Wolfe A.J., Parikh N., Lima B.P., and Zemaitaitis B. Signal integration by the two-component signal transduction response regulator CpxR. J. Bacteriol. 190 (2008) 2314-2322
    • (2008) J. Bacteriol. , vol.190 , pp. 2314-2322
    • Wolfe, A.J.1    Parikh, N.2    Lima, B.P.3    Zemaitaitis, B.4
  • 61
    • 0024219910 scopus 로고
    • EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro
    • Igo M.M., and Silhavy T.J. EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro. J. Bacteriol. 170 (1988) 5971-5973
    • (1988) J. Bacteriol. , vol.170 , pp. 5971-5973
    • Igo, M.M.1    Silhavy, T.J.2
  • 62
    • 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., and Kenney L.J. C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc. Natl Acad. Sci. USA 96 (1999) 11792-11797
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenney, L.J.3
  • 63
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary W.R., and Stock J.B. Acetyl phosphate and the activation of two-component response regulators. J. Biol. Chem. 269 (1994) 31567-31572
    • (1994) J. Biol. Chem. , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 64
    • 0036886272 scopus 로고    scopus 로고
    • Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator
    • Yoshida T., Cai S., and Inouye M. Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator. Mol. Microbiol. 46 (2002) 1283-1294
    • (2002) Mol. Microbiol. , vol.46 , pp. 1283-1294
    • Yoshida, T.1    Cai, S.2    Inouye, M.3
  • 65
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in Escherichia coli
    • Cai S.J., and Inouye M. EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J. Biol. Chem. 277 (2002) 24155-24161
    • (2002) J. Biol. Chem. , vol.277 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 67
    • 0025117574 scopus 로고
    • Evidence for multiple OmpR-binding sites in the upstream activation sequence of the ompC promoter in Escherichia coli: a single OmpR-binding site is capable of activating the promoter
    • Maeda S., and Mizuno T. Evidence for multiple OmpR-binding sites in the upstream activation sequence of the ompC promoter in Escherichia coli: a single OmpR-binding site is capable of activating the promoter. J. Bacteriol. 172 (1990) 501-503
    • (1990) J. Bacteriol. , vol.172 , pp. 501-503
    • Maeda, S.1    Mizuno, T.2
  • 68
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • Yamamoto K., and Ishihama A. Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci., Biotechnol., Biochem. 70 (2006) 1688-1695
    • (2006) Biosci., Biotechnol., Biochem. , vol.70 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2
  • 69
    • 7744235343 scopus 로고    scopus 로고
    • Continuous control in bacterial regulatory circuits
    • Batchelor E., Silhavy T.J., and Goulian M. Continuous control in bacterial regulatory circuits. J. Bacteriol. 186 (2004) 7618-7625
    • (2004) J. Bacteriol. , vol.186 , pp. 7618-7625
    • Batchelor, E.1    Silhavy, T.J.2    Goulian, M.3
  • 70
    • 0037133315 scopus 로고    scopus 로고
    • Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway
    • Otto K., and Silhavy T.J. Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway. Proc. Natl Acad. Sci. USA 99 (2002) 2287-2292
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2287-2292
    • Otto, K.1    Silhavy, T.J.2
  • 71
    • 33645468730 scopus 로고    scopus 로고
    • Imaging OmpR localization in Escherichia coli
    • Batchelor E., and Goulian M. Imaging OmpR localization in Escherichia coli. Mol. Microbiol. 59 (2006) 1767-1778
    • (2006) Mol. Microbiol. , vol.59 , pp. 1767-1778
    • Batchelor, E.1    Goulian, M.2
  • 72
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: how one organism sees its world
    • Fabret C., Feher A., and Hoch J.A. Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J. Bacteriol. 181 (1999) 1975-1983
    • (1999) J. Bacteriol. , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, A.2    Hoch, J.A.3
  • 73
    • 0033711144 scopus 로고    scopus 로고
    • Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis
    • Jiang M., Shao W., Perego M., and Hoch J.A. Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis. Mol. Microbiol. 38 (2000) 535-542
    • (2000) Mol. Microbiol. , vol.38 , pp. 535-542
    • Jiang, M.1    Shao, W.2    Perego, M.3    Hoch, J.A.4
  • 74
    • 0043032929 scopus 로고    scopus 로고
    • Phenotype microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems
    • Zhou L., Lei X.H., Bochner B.R., and Wanner B.L. Phenotype microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems. J. Bacteriol. 185 (2003) 4956-4972
    • (2003) J. Bacteriol. , vol.185 , pp. 4956-4972
    • Zhou, L.1    Lei, X.H.2    Bochner, B.R.3    Wanner, B.L.4
  • 75
    • 14644435718 scopus 로고    scopus 로고
    • CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli
    • Jubelin G., Vianney A., Beloin C., Ghigo J.M., Lazzaroni J.C., Lejeune P., and Dorel C. CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli. J. Bacteriol. 187 (2005) 2038-2049
    • (2005) J. Bacteriol. , vol.187 , pp. 2038-2049
    • Jubelin, G.1    Vianney, A.2    Beloin, C.3    Ghigo, J.M.4    Lazzaroni, J.C.5    Lejeune, P.6    Dorel, C.7
  • 76
    • 0036033707 scopus 로고    scopus 로고
    • Transcriptome analysis of all two-component regulatory system mutants of Escherichia coli K-12
    • Oshima T., Aiba H., Masuda Y., Kanaya S., Sugiura M., Wanner B.L., et al. Transcriptome analysis of all two-component regulatory system mutants of Escherichia coli K-12. Mol. Microbiol. 46 (2002) 281-291
    • (2002) Mol. Microbiol. , vol.46 , pp. 281-291
    • Oshima, T.1    Aiba, H.2    Masuda, Y.3    Kanaya, S.4    Sugiura, M.5    Wanner, B.L.6
  • 77
    • 0037192777 scopus 로고    scopus 로고
    • Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ
    • Mattison K., and Kenney L.J. Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ. J. Biol. Chem. 277 (2002) 11143-11148
    • (2002) J. Biol. Chem. , vol.277 , pp. 11143-11148
    • Mattison, K.1    Kenney, L.J.2
  • 78
    • 33748953866 scopus 로고    scopus 로고
    • Genetic parts to program bacteria
    • Voigt C.A. Genetic parts to program bacteria. Curr. Opin. Biotechnol. 17 (2006) 548-557
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 548-557
    • Voigt, C.A.1
  • 79
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 81
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., and Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl Acad. Sci. USA 97 (2000) 6640-6645
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.