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Volumn 331, Issue 4, 2003, Pages 941-949

Transmembrane organization of the Bacillus subtilis chemoreceptor McpB deduced by cysteine disulfide crosslinking

Author keywords

Chemoreceptor; Chemotaxis; Crosslinking; Helix packing; Structure

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DISULFIDE; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; MONOMER; PHOSPHOTRANSFERASE;

EID: 0042667015     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00834-9     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke J.J., Hazelbauer G.L. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26:2001;257-265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 2
    • 0027175202 scopus 로고
    • The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding
    • Yeh J.I., Biemann H.P., Pandit J., Koshland D.E., Kim S.H. The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J. Biol. Chem. 268:1993;9787-9792.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9787-9792
    • Yeh, J.I.1    Biemann, H.P.2    Pandit, J.3    Koshland, D.E.4    Kim, S.H.5
  • 3
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim K.K., Yokota H., Kim S.H. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature. 400:1999;787-792.
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.H.3
  • 4
    • 0028290945 scopus 로고
    • The serine receptor of bacterial chemotaxis exhibits half-site saturation for serine binding
    • Lin L.N., Li J., Brandts J.F., Weis R.M. The serine receptor of bacterial chemotaxis exhibits half-site saturation for serine binding. Biochemistry. 33:1994;6564-6570.
    • (1994) Biochemistry , vol.33 , pp. 6564-6570
    • Lin, L.N.1    Li, J.2    Brandts, J.F.3    Weis, R.M.4
  • 5
    • 0028924963 scopus 로고
    • Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo
    • Lee G.F., Lebert M.R., Lilly A.A., Hazelbauer G.L. Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo. Proc. Natl Acad. Sci. USA. 92:1995;3391-3395.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3391-3395
    • Lee, G.F.1    Lebert, M.R.2    Lilly, A.A.3    Hazelbauer, G.L.4
  • 6
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann K.M., Xiao W., Shin Y.K., Koshland D.E. Jr. A piston model for transmembrane signaling of the aspartate receptor. Science. 285:1999;1751-1754.
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland D.E., Jr.4
  • 8
    • 0033931244 scopus 로고    scopus 로고
    • Structure of a conserved receptor domain that regulates kinase activity: The cytoplasmic domain of bacterial taxis receptors
    • Falke J.J., Kim S.H. Structure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors. Curr. Opin. Struct. Biol. 10:2000;462-469.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 462-469
    • Falke, J.J.1    Kim, S.H.2
  • 9
    • 0030905518 scopus 로고    scopus 로고
    • Methanol production during chemotaxis to amino acids in Bacillus subtilis
    • Kirby J.R., Kristich C.J., Feinberg S.L., Ordal G.W. Methanol production during chemotaxis to amino acids in Bacillus subtilis. Mol. Microbiol. 24:1997;869-878.
    • (1997) Mol. Microbiol. , vol.24 , pp. 869-878
    • Kirby, J.R.1    Kristich, C.J.2    Feinberg, S.L.3    Ordal, G.W.4
  • 10
    • 0025107949 scopus 로고
    • Methyl group turnover on methyl-accepting chemotaxis proteins during chemotaxis by Bacillus subtilis
    • Thoelke M.S., Casper J.M., Ordal G.W. Methyl group turnover on methyl-accepting chemotaxis proteins during chemotaxis by Bacillus subtilis. J. Biol. Chem. 265:1990;1928-1932.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1928-1932
    • Thoelke, M.S.1    Casper, J.M.2    Ordal, G.W.3
  • 11
    • 0021162295 scopus 로고
    • Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli
    • Kehry M.R., Doak T.G., Dahlquist F.W. Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli. J. Biol. Chem. 259:1984;11828-11835.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11828-11835
    • Kehry, M.R.1    Doak, T.G.2    Dahlquist, F.W.3
  • 12
    • 0018800404 scopus 로고
    • Methanol formation in vivo from methylated chemotaxis proteins in Escherichia coli
    • Toews M.L., Adler J. Methanol formation in vivo from methylated chemotaxis proteins in Escherichia coli. J. Biol. Chem. 254:1979;1761-1764.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1761-1764
    • Toews, M.L.1    Adler, J.2
  • 13
    • 0023752188 scopus 로고
    • Rapid attractant-induced changes in methylation of methyl-accepting chemotaxis proteins in Bacillus subtilis
    • Thoelke M.S., Parker H.M., Ordal E.A., Ordal G.W. Rapid attractant-induced changes in methylation of methyl-accepting chemotaxis proteins in Bacillus subtilis. Biochemistry. 27:1988;8453-8457.
    • (1988) Biochemistry , vol.27 , pp. 8453-8457
    • Thoelke, M.S.1    Parker, H.M.2    Ordal, E.A.3    Ordal, G.W.4
  • 14
    • 0034637533 scopus 로고    scopus 로고
    • Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation
    • Zimmer M.A., Tiu J., Collins M.A., Ordal G.W. Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation. J. Biol. Chem. 275:2000;24264-24272.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24264-24272
    • Zimmer, M.A.1    Tiu, J.2    Collins, M.A.3    Ordal, G.W.4
  • 15
    • 0026664405 scopus 로고
    • Attenuation of sensory receptor signaling by covalent modification
    • Borkovich K.A., Alex L.A., Simon M.I. Attenuation of sensory receptor signaling by covalent modification. Proc. Natl Acad. Sci. USA. 89:1992;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
  • 16
    • 0026031833 scopus 로고
    • Tuning the responsiveness of a sensory receptor via covalent modification
    • Dunten P., Koshland D.E. Jr. Tuning the responsiveness of a sensory receptor via covalent modification. J. Biol. Chem. 266:1991;1491-1496.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1491-1496
    • Dunten, P.1    Koshland D.E., Jr.2
  • 17
    • 0017759615 scopus 로고
    • Sensory transduction in Escherichia coli: Role of a protein methylation reaction in sensory adaptation
    • Goy M.F., Springer M.S., Adler J. Sensory transduction in Escherichia coli: role of a protein methylation reaction in sensory adaptation. Proc. Natl Acad. Sci. USA. 74:1977;4964-4968.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 4964-4968
    • Goy, M.F.1    Springer, M.S.2    Adler, J.3
  • 18
    • 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., Koshland D.E. Jr. Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J. Mol. Biol. 261:1996;568-585.
    • (1996) J. Mol. Biol. , vol.261 , pp. 568-585
    • Le Moual, H.1    Koshland D.E., Jr.2
  • 19
    • 0028336799 scopus 로고
    • Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis
    • Hanlon D.W., Ordal G.W. Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis. J. Biol. Chem. 269:1994;14038-14046.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14038-14046
    • Hanlon, D.W.1    Ordal, G.W.2
  • 20
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg
    • Lee G.F., Burrows G.G., Lebert M.R., Dutton D.P., Hazelbauer G.L. Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg. J. Biol. Chem. 269:1994;29920-29927.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 21
    • 0023224051 scopus 로고
    • Global flexibility in a sensory receptor: A site-directed cross-linking approach
    • Falke J.J., Koshland D.E. Jr. Global flexibility in a sensory receptor: a site-directed cross-linking approach. Science. 237:1987;1596-1600.
    • (1987) Science , vol.237 , pp. 1596-1600
    • Falke, J.J.1    Koshland D.E., Jr.2
  • 22
    • 0036069314 scopus 로고    scopus 로고
    • The role of heterologous receptors in McpB-mediated signalling in Bacillus subtilis chemotaxis
    • Zimmer M.A., Szurmant H., Saulmon M.M., Collins M.A., Bant J.S., Ordal G.W. The role of heterologous receptors in McpB-mediated signalling in Bacillus subtilis chemotaxis. Mol. Microbiol. 45:2002;555-568.
    • (2002) Mol. Microbiol. , vol.45 , pp. 555-568
    • Zimmer, M.A.1    Szurmant, H.2    Saulmon, M.M.3    Collins, M.A.4    Bant, J.S.5    Ordal, G.W.6
  • 23
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli
    • Lynch B.A., Koshland D.E. Jr. Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. Proc. Natl Acad. Sci. USA. 88:1991;10402-10406.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland D.E., Jr.2
  • 24
    • 0027194322 scopus 로고
    • Chemotactic methylesterase promotes adaptation to high concentrations of attractant in Bacillus subtilis
    • Kirsch M.L., Peters P.D., Hanlon D.W., Kirby J.R., Ordal G.W. Chemotactic methylesterase promotes adaptation to high concentrations of attractant in Bacillus subtilis. J. Biol. Chem. 268:1993;18610-18616.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18610-18616
    • Kirsch, M.L.1    Peters, P.D.2    Hanlon, D.W.3    Kirby, J.R.4    Ordal, G.W.5
  • 25
    • 0027381347 scopus 로고
    • Chemotactic methyltransferase promotes adaptation to repellents in Bacillus subtilis
    • Kirsch M.L., Zuberi A.R., Henner D., Peters P.D., Yazdi M.A., Ordal G.W. Chemotactic methyltransferase promotes adaptation to repellents in Bacillus subtilis. J. Biol. Chem. 268:1993;25350-25356.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25350-25356
    • Kirsch, M.L.1    Zuberi, A.R.2    Henner, D.3    Peters, P.D.4    Yazdi, M.A.5    Ordal, G.W.6
  • 26
    • 0033963325 scopus 로고    scopus 로고
    • CheB is required for behavioural responses to negative stimuli during chemotaxis in Bacillus subtilis
    • Kirby J.R., Niewold T.B., Maloy S., Ordal G.W. CheB is required for behavioural responses to negative stimuli during chemotaxis in Bacillus subtilis. Mol. Microbiol. 35:2000;44-57.
    • (2000) Mol. Microbiol. , vol.35 , pp. 44-57
    • Kirby, J.R.1    Niewold, T.B.2    Maloy, S.3    Ordal, G.W.4
  • 29
    • 0031767491 scopus 로고    scopus 로고
    • Stimulus response coupling in bacterial chemotaxis: Receptor dimers in signalling arrays
    • Levit M.N., Liu Y., Stock J.B. Stimulus response coupling in bacterial chemotaxis: receptor dimers in signalling arrays. Mol. Microbiol. 30:1998;459-466.
    • (1998) Mol. Microbiol. , vol.30 , pp. 459-466
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 30
    • 0037015003 scopus 로고    scopus 로고
    • Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity
    • Kim S.H., Wang W., Kim K.K. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity. Proc. Natl Acad. Sci. USA. 99:2002;11611-11615.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11611-11615
    • Kim, S.H.1    Wang, W.2    Kim, K.K.3
  • 31
    • 0037076381 scopus 로고    scopus 로고
    • Cooperativity between bacterial chemotaxis receptors
    • Falke J.J. Cooperativity between bacterial chemotaxis receptors. Proc. Natl Acad. Sci. USA. 99:2002;6530-6532.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 6530-6532
    • Falke, J.J.1
  • 32
    • 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., Stock J.B. Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J. 16:1997;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
  • 33
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock J.R., Shapiro L. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science. 259:1993;1717-1723.
    • (1993) Science , vol.259 , pp. 1717-1723
    • Maddock, J.R.1    Shapiro, L.2
  • 34
    • 0034603209 scopus 로고    scopus 로고
    • Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli
    • Li G., Weis R.M. Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell. 100:2000;357-365.
    • (2000) Cell , vol.100 , pp. 357-365
    • Li, G.1    Weis, R.M.2
  • 35
    • 0037184003 scopus 로고    scopus 로고
    • Organization of the receptor-kinase signaling array that regulates E. coli chemotaxis
    • Levit M.N., Grebe T.W., Stock J.B. Organization of the receptor-kinase signaling array that regulates E. coli chemotaxis. J. Biol. Chem. 277:2002;36748-36754.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36748-36754
    • Levit, M.N.1    Grebe, T.W.2    Stock, J.B.3
  • 36
    • 0033565446 scopus 로고    scopus 로고
    • The aspartate receptor cytoplasmic domain: In situ chemical analysis of structure, mechanism and dynamics
    • Bass R.B., Falke J.J. The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics. Struct. Fold. Des. 7:1999;829-840.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 829-840
    • Bass, R.B.1    Falke, J.J.2
  • 37
    • 0035168279 scopus 로고    scopus 로고
    • CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis
    • Kirby J.R., Kristich C.J., Saulmon M.M., Zimmer M.A., Garrity L.F., Zhulin I.B., Ordal G.W. CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis. Mol. Microbiol. 42:2001;573-585.
    • (2001) Mol. Microbiol. , vol.42 , pp. 573-585
    • Kirby, J.R.1    Kristich, C.J.2    Saulmon, M.M.3    Zimmer, M.A.4    Garrity, L.F.5    Zhulin, I.B.6    Ordal, G.W.7
  • 38
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and Bacteria
    • Hou S., Larsen R.W., Boudko D., Riley C.W., Karatan E., Zimmer M., et al. Myoglobin-like aerotaxis transducers in Archaea and Bacteria. Nature. 403:2000;540-544.
    • (2000) Nature , vol.403 , pp. 540-544
    • Hou, S.1    Larsen, R.W.2    Boudko, D.3    Riley, C.W.4    Karatan, E.5    Zimmer, M.6
  • 39
    • 0037067781 scopus 로고    scopus 로고
    • Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis
    • Kristich C.J., Ordal G.W. Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis. J. Biol. Chem. 277:2002;25356-25362.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25356-25362
    • Kristich, C.J.1    Ordal, G.W.2
  • 40
    • 0028333653 scopus 로고
    • Chemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologs
    • Rosario M.M., Fredrick K.L., Ordal G.W., Helmann J.D. Chemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologs. J. Bacteriol. 176:1994;2736-2739.
    • (1994) J. Bacteriol. , vol.176 , pp. 2736-2739
    • Rosario, M.M.1    Fredrick, K.L.2    Ordal, G.W.3    Helmann, J.D.4
  • 41
    • 0040822641 scopus 로고    scopus 로고
    • Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis
    • Muller J., Schiel S., Ordal G.W., Saxild H.H. Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis. Microbiology. 143:1997;3231-3240.
    • (1997) Microbiology , vol.143 , pp. 3231-3240
    • Muller, J.1    Schiel, S.2    Ordal, G.W.3    Saxild, H.H.4
  • 42
    • 0019422223 scopus 로고
    • In vivo and in vitro chemotactic methylation in Bacillus subtilis
    • Ullah A.H., Ordal G.W. In vivo and in vitro chemotactic methylation in Bacillus subtilis. J. Bacteriol. 145:1981;958-965.
    • (1981) J. Bacteriol. , vol.145 , pp. 958-965
    • Ullah, A.H.1    Ordal, G.W.2
  • 43
    • 0037340214 scopus 로고    scopus 로고
    • The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis
    • Kristich C.J., Glekas G.D., Ordal G.W. The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis. Mol. Microbiol. 47:2003;1353-1366.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1353-1366
    • Kristich, C.J.1    Glekas, G.D.2    Ordal, G.W.3


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