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Volumn 9, Issue 2, 1999, Pages 115-118

Bacterial Chemoreceptors: Recent Progress in Structure and Function

Author keywords

Chemotaxis; Conformational Changes; Periplasmic Binding Proteins; Receptor; Signaling

Indexed keywords

BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; TAR PROTEIN, E COLI;

EID: 0033616994     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (9)

References (32)
  • 1
    • 0026664405 scopus 로고
    • Attenuation of sensory receptor signaling by covalent modification
    • Borkovich, K. A., Alex, L. A., and Simon, M. I. (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
  • 2
    • 0028818765 scopus 로고
    • Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor
    • Chervitz, S. A. and Falke, J. J. (1995) Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor. J. Biol. Chem. 270, 24043-24053.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24043-24053
    • Chervitz, S.A.1    Falke, J.J.2
  • 3
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz, S. A. and Falke, J. J. (1996) Molecular mechanism of transmembrane signaling by the aspartate receptor: a model. Proc. Natl. Acad. Sci. USA 93, 2545-2550.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 4
    • 0031451150 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor
    • Danielson, M. A., Bass, R. B., and Falke, J. J. (1997) Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor. J. Biol. Chem. 272, 32878-32888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32878-32888
    • Danielson, M.A.1    Bass, R.B.2    Falke, J.J.3
  • 5
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • Djordjevic, S., Goudreau, P. N., Xu, Q., Stock, A. M., and West, A. H. (1998) Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc. Natl. Acad. Sci. USA 95, 1381-1386.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1381-1386
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 6
    • 0031749947 scopus 로고    scopus 로고
    • Chemotaxis receptor recognition by protein methyltransferase CheR
    • Djordjevic, S. and Stock, A. M. (1998) Chemotaxis receptor recognition by protein methyltransferase CheR. Nature Struct. Biol. 5, 446-450.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 446-450
    • Djordjevic, S.1    Stock, A.M.2
  • 7
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke, J. J., Bass, R. B., Butler, S. L., Chervitz, S. A., and Danielson, M. A. (1997) The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol. 13, 457-512.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 8
    • 0030971441 scopus 로고    scopus 로고
    • Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor
    • Gardina, P. J., Bormans, A. F., Hawkins, M. A., Meeker, J. W., and Manson, M. D. (1997) Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor. Mol. Microbiol. 23, 1181-1191.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1181-1191
    • Gardina, P.J.1    Bormans, A.F.2    Hawkins, M.A.3    Meeker, J.W.4    Manson, M.D.5
  • 9
    • 0026808410 scopus 로고
    • Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
    • Gegner, J. A., Graham, D. R., Roth, A. F., and Dahlquist, F. W. (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
  • 10
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C.-H. (1995) Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 11
    • 0030606898 scopus 로고    scopus 로고
    • Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis
    • Le Moual, H. and Koshland, D. E. Jr. (1996) Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J. Mol. Biol. 261, 568-585.
    • (1996) J. Mol. Biol. , vol.261 , pp. 568-585
    • Le Moual, H.1    Koshland D.E., Jr.2
  • 12
    • 0030736078 scopus 로고    scopus 로고
    • Methylation of the Escherichia coli chemotaxis receptors: Intra- and interdimer mechanisms
    • Le Moual, H., Quang, T., and Koshland, D. E. Jr. (1997) Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 36, 13441-13448.
    • (1997) Biochemistry , vol.36 , pp. 13441-13448
    • Le Moual, H.1    Quang, T.2    Koshland D.E., Jr.3
  • 13
    • 0030768758 scopus 로고    scopus 로고
    • The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process
    • Li, J., Li, G., and Weis, R. M. (1997) The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process. Biochemistry 36, 11851-11857.
    • (1997) Biochemistry , vol.36 , pp. 11851-11857
    • Li, J.1    Li, G.2    Weis, R.M.3
  • 14
    • 0031449028 scopus 로고    scopus 로고
    • Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis
    • Liu, Y., Levit, M., Lurz, R., Surette, M. G., and Stock, J. B. (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
  • 15
    • 0024347198 scopus 로고
    • Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chernotaxis
    • Lupas, A. and Stock, J. (1989) Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chernotaxis. J. Biol. Chem. 264, 17337-17342.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17337-17342
    • Lupas, A.1    Stock, J.2
  • 16
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., van Dyke, M., and Stock, J. (1991) Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 17
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli
    • Lynch, B. A. and Koshland, D. E. Jr. (1991) Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. Proc. Natl. Acad. Sci. USA 88, 10402-10406.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland D.E., Jr.2
  • 18
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock, J. R. and Shapiro, L. (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
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M., Priv, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E. Jr., and Kim, S.-H. (1991) Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254, 1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.1    Priv, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland D.E., Jr.7    Kim, S.-H.8
  • 20
    • 0023917333 scopus 로고
    • Site-directed cross-linking: Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis
    • Milligan, D. L. and Koshland, D. E. Jr. (1988) Site-directed cross-linking: Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J. Biol. Chem. 263, 6268-6275.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6268-6275
    • Milligan, D.L.1    Koshland D.E., Jr.2
  • 21
    • 0027248998 scopus 로고
    • Purification and characterization of the periplasmic domain of the aspartate chemoreceptor
    • Milligan, D. L. and Koshland, D. E. Jr. (1993) Purification and characterization of the periplasmic domain of the aspartate chemoreceptor. J. Biol. Chem. 268, 19991-19997.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19991-19997
    • Milligan, D.L.1    Koshland D.E., Jr.2
  • 22
    • 0022179404 scopus 로고
    • Proteolytic fragments identified with domains of the aspartate chemoreceptor
    • Mowbray, S. L., Foster, D. L., and Koshland, D. E. Jr. (1985) Proteolytic fragments identified with domains of the aspartate chemoreceptor. J. Biol. Chem. 260, 11711-11718.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11711-11718
    • Mowbray, S.L.1    Foster, D.L.2    Koshland D.E., Jr.3
  • 23
    • 0025830353 scopus 로고
    • Reconstitution of the bacterial chemotaxis signal transduction system from purified components
    • Ninfa, E. G., Stock, A., Mowbray, S. L., and Stock, J. (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.L.3    Stock, J.4
  • 24
    • 0020625608 scopus 로고
    • Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing
    • Russo, A. F. and Koshland, D. E. Jr. (1983) Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing. Science 220, 1016-1020.
    • (1983) Science , vol.220 , pp. 1016-1020
    • Russo, A.F.1    Koshland D.E., Jr.2
  • 25
    • 0029970581 scopus 로고    scopus 로고
    • The cytoplasmic fragment of the aspartate receptor displays globally dynamic behavior
    • Seeley, S. K., Weis, R. M., and Thompson, L. K. (1996) The cytoplasmic fragment of the aspartate receptor displays globally dynamic behavior. Biochemistry 35, 5199-5206.
    • (1996) Biochemistry , vol.35 , pp. 5199-5206
    • Seeley, S.K.1    Weis, R.M.2    Thompson, L.K.3
  • 26
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chernotaxis
    • Sharff, A. J., Rodseth, L. E., Spurlino, J. C., and Quiocho, F. A. (1992) Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chernotaxis. Biochemistry 31, 10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 27
    • 0022405719 scopus 로고
    • Multiple forms of the CheB methylesterase in bacterial chemosensing
    • Simms, S. A., Keane, M. G., and Stock, J. (1985) Multiple forms of the CheB methylesterase in bacterial chemosensing. J. Biol. Chem. 260, 10161-10168.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10161-10168
    • Simms, S.A.1    Keane, M.G.2    Stock, J.3
  • 28
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose- Or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y., and Quiocho, F. A. (1991) The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 29
    • 0025805549 scopus 로고
    • Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks
    • Stock, J. B., Lukat, G., and Stock, A. M. (1991) Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. Annu. Rev. Biophys. Biophys. Chem. 20, 109-136.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 109-136
    • Stock, J.B.1    Lukat, G.2    Stock, A.M.3
  • 30
    • 0000621729 scopus 로고    scopus 로고
    • Chemotaxis
    • Niedhart, F., Ingraham, R. C., Lin, E., Low, K., Magasanik, B., Reznikoff, W., Riley, M., Schaechter, M., and Umbarger, H., (eds.), American Society for Microbiology Press, Washington, D.C.
    • Stock, J. B. and Surette, M. G. (1996) Chemotaxis; in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd ed., Niedhart, F., Ingraham, R. C., Lin, E., Low, K., Magasanik, B., Reznikoff, W., Riley, M., Schaechter, M., and Umbarger, H., (eds.), pp. 1103-1129, American Society for Microbiology Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology, 2nd Ed. , pp. 1103-1129
    • Stock, J.B.1    Surette, M.G.2
  • 31
    • 0029979271 scopus 로고    scopus 로고
    • The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation
    • Wu, J., Li, J., Li, G., Long, D. G., and Weis, R. M (1996) The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation. Biochemistry 35, 4984-4993.
    • (1996) Biochemistry , vol.35 , pp. 4984-4993
    • Wu, J.1    Li, J.2    Li, G.3    Long, D.G.4    Weis, R.M.5


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