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Volumn 186, Issue 19, 2004, Pages 6643-6646

Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME;

EID: 4544327632     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.19.6643-6646.2004     Document Type: Article
Times cited : (44)

References (26)
  • 1
    • 2142753979 scopus 로고    scopus 로고
    • Dynamic receptor team formation can explain the high signal transduction gain in Escherichia coli
    • Albert, R., Y. W. Chiu, and H. G. Othmer. 2004. Dynamic receptor team formation can explain the high signal transduction gain in Escherichia coli. Biophys. J. 86:2650-2659.
    • (2004) Biophys. J. , vol.86 , pp. 2650-2659
    • Albert, R.1    Chiu, Y.W.2    Othmer, H.G.3
  • 2
  • 3
    • 0026664405 scopus 로고
    • Attenuation of sensory receptor signaling by covalent modification
    • Borkovich, K. A., L. A. Alex, and M. I. Simon. 1992. Attenuation of sensory receptor signaling by covalent modification. Proc. Natl. Acad. Sci. USA 89:6756-6760.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6756-6760
    • Borkovich, K.A.1    Alex, L.A.2    Simon, M.I.3
  • 4
    • 0006611890 scopus 로고
    • Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer
    • Borkovich, K. A., N. Kaplan, J. F. Hess, and M. I. Simon. 1989. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Natl. Acad. Sci. USA 86:1208-1212.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1208-1212
    • Borkovich, K.A.1    Kaplan, N.2    Hess, J.F.3    Simon, M.I.4
  • 5
    • 0034622634 scopus 로고    scopus 로고
    • Attractant regulation of the aspartate receptor-kinase complex: Limited cooperative interactions between receptors and effects of the receptor modification state
    • Bornhorst, J. A., and J. J. Falke. 2000. Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state. Biochemistry 39:9486-9493.
    • (2000) Biochemistry , vol.39 , pp. 9486-9493
    • Bornhorst, J.A.1    Falke, J.J.2
  • 6
    • 0037424604 scopus 로고    scopus 로고
    • Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: Development of a heterogeneous two-state model
    • Bornhorst, J. A., and J. J. Falke. 2003. Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model. J. Mol. Biol. 326:1597-1614.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1597-1614
    • Bornhorst, J.A.1    Falke, J.J.2
  • 7
    • 0037151097 scopus 로고    scopus 로고
    • CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli
    • Boukhvalova, M. S., F. W. Dahlquist, and R. C. Stewart. 2002. CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli. J. Biol. Chem. 277:22251-22259.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22251-22259
    • Boukhvalova, M.S.1    Dahlquist, F.W.2    Stewart, R.C.3
  • 9
    • 0018712142 scopus 로고
    • Membrane receptors for aspartate and serine in bacterial chemotaxis
    • Clarke, S., and D. E. Koshland, Jr. 1979. Membrane receptors for aspartate and serine in bacterial chemotaxis. J. Biol. Chem. 254:9695-9702.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9695-9702
    • Clarke, S.1    Koshland Jr., D.E.2
  • 10
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J., and G. L. Hazelbauer. 2001. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26:257-265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 11
    • 0026808410 scopus 로고
    • Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
    • Gegner, J. A., D. R. Graham, A. F. Roth, and F. W. Dahlquist. 1992. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 70:975-982.
    • (1992) Cell , vol.70 , pp. 975-982
    • Gegner, J.A.1    Graham, D.R.2    Roth, A.F.3    Dahlquist, F.W.4
  • 12
    • 0026062038 scopus 로고
    • Tandem translation starts in the cheA locus of Escherichia coli
    • Kofoid, E. C., and J. S. Parkinson. 1991. Tandem translation starts in the cheA locus of Escherichia coli. J. Bacteriol. 173:2116-2119.
    • (1991) J. Bacteriol. , vol.173 , pp. 2116-2119
    • Kofoid, E.C.1    Parkinson, J.S.2
  • 13
    • 0037184003 scopus 로고    scopus 로고
    • Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis
    • Levit, M. N., T. W. Grebe, and J. B. Stock. 2002. Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis. J. Biol. Chem. 277:36748-36754.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36748-36754
    • Levit, M.N.1    Grebe, T.W.2    Stock, J.B.3
  • 14
    • 0037184120 scopus 로고    scopus 로고
    • Receptor methylation controls the magnitude of stimulus-response coupling in bacterial chemotaxis
    • Levit, M. N., and J. B. Stock. 2002. Receptor methylation controls the magnitude of stimulus-response coupling in bacterial chemotaxis. J. Biol. Chem. 277:36760-36765.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36760-36765
    • Levit, M.N.1    Stock, J.B.2
  • 15
    • 0034603209 scopus 로고    scopus 로고
    • Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli
    • Li, G., and R. M. Weis. 2000. Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell 100:357-365.
    • (2000) Cell , vol.100 , pp. 357-365
    • Li, G.1    Weis, R.M.2
  • 16
    • 0031449028 scopus 로고    scopus 로고
    • Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis
    • Liu, Y, M. Levit, R. Lurz, M. G. Surette, and J. B. Stock. 1997. Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J. 16:7231-7240.
    • (1997) EMBO J. , vol.16 , pp. 7231-7240
    • Liu, Y.1    Levit, M.2    Lurz, R.3    Surette, M.G.4    Stock, J.B.5
  • 17
    • 0032884359 scopus 로고    scopus 로고
    • Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB
    • Lybarger, S. R., and J. R. Maddock. 1999. Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB. J. Bacteriol. 181:5527-5529.
    • (1999) J. Bacteriol. , vol.181 , pp. 5527-5529
    • Lybarger, S.R.1    Maddock, J.R.2
  • 18
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock, J. R., and L. Shapiro. 1993. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259:1717-1723.
    • (1993) Science , vol.259 , pp. 1717-1723
    • Maddock, J.R.1    Shapiro, L.2
  • 19
    • 0025830353 scopus 로고
    • Reconstitution of the bacterial chemotaxis signal transduction system from purified components
    • Ninfa, E. G., A. Stock, S. Mowbray, and J. B. Stock. 1991. Reconstitution of the bacterial chemotaxis signal transduction system from purified components. J. Biol. Chem. 266:9764-9770.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9764-9770
    • Ninfa, E.G.1    Stock, A.2    Mowbray, S.3    Stock, J.B.4
  • 20
    • 0019979301 scopus 로고
    • Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions
    • Parkinson, J. S., and S. E. Houts. 1982. Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions. J. Bacteriol. 151:106-113.
    • (1982) J. Bacteriol. , vol.151 , pp. 106-113
    • Parkinson, J.S.1    Houts, S.E.2
  • 21
    • 0036830605 scopus 로고    scopus 로고
    • Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase
    • Shiomi, D., I. B. Zhulin, M. Homma, and I. Kawagishi. 2002. Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase. J. Biol. Chem. 277:42325-42333.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42325-42333
    • Shiomi, D.1    Zhulin, I.B.2    Homma, M.3    Kawagishi, I.4
  • 22
    • 0345686458 scopus 로고    scopus 로고
    • Template-directed assembly of receptor signaling complexes
    • Shrout, A. L., D. J. Montefusco, and R. M. Weis. 2003. Template-directed assembly of receptor signaling complexes. Biochemistry 42:13379-13385.
    • (2003) Biochemistry , vol.42 , pp. 13379-13385
    • Shrout, A.L.1    Montefusco, D.J.2    Weis, R.M.3
  • 23
    • 0036790991 scopus 로고    scopus 로고
    • Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer
    • Sourjik, V., and H. C. Berg. 2002. Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 99:12669-12674.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12669-12674
    • Sourjik, V.1    Berg, H.C.2
  • 24
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik, V., and H. C. Berg. 2004. Functional interactions between receptors in bacterial chemotaxis. Nature 428:437-441.
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 25
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Esherichia coli using fluorescent protein fusions
    • Sourjik, V., and H. C. Berg. 2000. Localization of components of the chemotaxis machinery of Esherichia coli using fluorescent protein fusions. Mol. Microbiol. 37:740-751.
    • (2000) Mol. Microbiol. , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 26
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V., and H. C. Berg. 2002. Receptor sensitivity in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 99:123-127.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.