메뉴 건너뛰기




Volumn 286, Issue 4, 1999, Pages 1059-1074

A free-energy-based stochastic simulation of the Tar receptor complex

Author keywords

Bacterial chemotaxis; Conformational change; Free energy; Individual based modelling; Signalling complex

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN;

EID: 0033525474     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2535     Document Type: Article
Times cited : (104)

References (54)
  • 2
    • 0021724874 scopus 로고
    • Two-state model for bacterial chemoreceptor proteins. The role of multiple methylation
    • Asakura S., Honda H. Two-state model for bacterial chemoreceptor proteins. The role of multiple methylation. J. Mol. Biol. 176:1984;349-367.
    • (1984) J. Mol. Biol. , vol.176 , pp. 349-367
    • Asakura, S.1    Honda, H.2
  • 3
    • 0030797355 scopus 로고    scopus 로고
    • Robustness in simple biochemical networks
    • Barkai N., Leibler S. Robustness in simple biochemical networks. Nature. 387:1997;913-917.
    • (1997) Nature , vol.387 , pp. 913-917
    • Barkai, N.1    Leibler, S.2
  • 4
    • 0001180444 scopus 로고
    • Transient response to chemotactic stimuli in Escherichia coli
    • Berg H. C., Tedesco P. M. Transient response to chemotactic stimuli in Escherichia coli. Proc. Natl Acad. Sci. USA. 72:1975;3235-3239.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 3235-3239
    • Berg, H.C.1    Tedesco, P.M.2
  • 5
    • 0028089151 scopus 로고
    • Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-sites cooperativity
    • Biemann H.-P., Koshland D. E. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-sites cooperativity. Biochemistry. 33:1994;629-634.
    • (1994) Biochemistry , vol.33 , pp. 629-634
    • Biemann, H.-P.1    Koshland, D.E.2
  • 6
    • 0022896181 scopus 로고
    • Demethylation of bacterial chemoreceptors is inhibited by attractant stimulion in the complete absence of the regulatory domain of the demethylating enzyme
    • Borczuk A., Staub A., Stock J. Demethylation of bacterial chemoreceptors is inhibited by attractant stimulion in the complete absence of the regulatory domain of the demethylating enzyme. Biochem. Biophys. Res. Commun. 141:1986;918-923.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 918-923
    • Borczuk, A.1    Staub, A.2    Stock, J.3
  • 7
    • 0025647599 scopus 로고
    • The dynamics of protein phosphorylation in bacterial chemotaxis
    • Borkovich K. A., Simon M. I. The dynamics of protein phosphorylation in bacterial chemotaxis. Cell. 63:1990;1339-1348.
    • (1990) Cell , vol.63 , pp. 1339-1348
    • Borkovich, K.A.1    Simon, M.I.2
  • 8
    • 0006611890 scopus 로고
    • Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer
    • Borkovich K. A., Kaplan N., Hess J. F., Simon N. I. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Natl Acad. Sci USA. 86:1989;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, N.I.4
  • 9
    • 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
  • 10
    • 0025908814 scopus 로고
    • Signal transduction pathways involving protein phosphorylation in prokaryotes
    • Bourret R. B., Borkovich K. A., Simon M. I. Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu. Rev. Biochem. 60:1991;401-441.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 401-441
    • Bourret, R.B.1    Borkovich, K.A.2    Simon, M.I.3
  • 11
    • 0031804503 scopus 로고    scopus 로고
    • Signaling complexes: Biophysical constraints on intracellular communication
    • Bray D. Signaling complexes: biophysical constraints on intracellular communication. Annu. Rev. Biophys.Biomol. Struct. 27:1998;59-75.
    • (1998) Annu. Rev. Biophys.Biomol. Struct. , vol.27 , pp. 59-75
    • Bray, D.1
  • 12
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray D., Levin M. D., Morton-Firth C. J. Receptor clustering as a cellular mechanism to control sensitivity. Nature. 393:1998;85-88.
    • (1998) Nature , vol.393 , pp. 85-88
    • Bray, D.1    Levin, M.D.2    Morton-Firth, C.J.3
  • 13
    • 0018712142 scopus 로고
    • Membrane receptors for aspartate and serine in bacterial chemotaxis
    • Clarke S., Koshland D. E. Membrane receptors for aspartate and serine in bacterial chemotaxis. J. Biol. Chem. 254:1979;9695-9702.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9695-9702
    • Clarke, S.1    Koshland, D.E.2
  • 15
    • 0345535783 scopus 로고    scopus 로고
    • Control of bacterial chemotaxis
    • Eisenbach M. Control of bacterial chemotaxis. Mol. Microbiol. 4:1996;161-167.
    • (1996) Mol. Microbiol. , vol.4 , pp. 161-167
    • Eisenbach, M.1
  • 16
    • 0029851704 scopus 로고    scopus 로고
    • Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
    • Gardina P. J., Manson M. D. Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain. Science. 274:1996;425-426.
    • (1996) Science , vol.274 , pp. 425-426
    • Gardina, P.J.1    Manson, M.D.2
  • 17
    • 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., Dahlquist F. W. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell. 70:1992;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
  • 18
    • 0024573668 scopus 로고
    • Adaptational "crosstalk" and the crucial role of methylation in chemotactic migration by Escherichia coli
    • Hazelbauer G. L., Park C., Nowlin D. M. Adaptational "crosstalk" and the crucial role of methylation in chemotactic migration by Escherichia coli. Proc. Natl Acad. Sci. USA. 86:1989;1448-1452.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 1448-1452
    • Hazelbauer, G.L.1    Park, C.2    Nowlin, D.M.3
  • 19
    • 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
  • 22
    • 0024457468 scopus 로고
    • Multiple kinetic states for the flagellar motor switch
    • Kuo S. C., Koshland D. E. Jr. Multiple kinetic states for the flagellar motor switch. J. Bacteriol. 171:1989;6279-6287.
    • (1989) J. Bacteriol. , vol.171 , pp. 6279-6287
    • Kuo, S.C.1    Koshland D.E., Jr.2
  • 23
    • 0028869205 scopus 로고
    • The response regulators CheB and CheY exhibit competitive binding to the kinase CheA
    • Li J., Swanson R. V., Simon M. L., Weis R. M. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry. 36:1995;14626-14636.
    • (1995) Biochemistry , vol.36 , pp. 14626-14636
    • Li, J.1    Swanson, R.V.2    Simon, M.L.3    Weis, R.M.4
  • 24
    • 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
  • 25
    • 0025881094 scopus 로고
    • Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis
    • Lukat G. S., Lee B. H., Mottonen J. M., Stock A. M., Stock J. B. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J. Biol. Chem. 266:1991;8348-8354.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8348-8354
    • Lukat, G.S.1    Lee, B.H.2    Mottonen, J.M.3    Stock, A.M.4    Stock, J.B.5
  • 26
    • 0024347198 scopus 로고
    • Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis
    • Lupas A., Stock J. Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J. Biol. Chem. 264:1989;17337-17342.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17337-17342
    • Lupas, A.1    Stock, J.2
  • 27
    • 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
  • 28
    • 0010418656 scopus 로고
    • Signalling complexes in bacterial chemotaxis
    • J. P. Armitage, & J. M. Lackie. Cambridge: Cambridge University Press
    • Matsumura P., Roman S., Volz K., McNally D. Signalling complexes in bacterial chemotaxis. Armitage J. P., Lackie J. M. Biology of the Chemotactic Response. 1990;Cambridge University Press, Cambridge.
    • (1990) Biology of the Chemotactic Response
    • Matsumura, P.1    Roman, S.2    Volz, K.3    McNally, D.4
  • 29
    • 0015845216 scopus 로고
    • The range of attractant concentrations for bacterial chemotaxis and the threshold and size of response over this range. Weber law and related phenomena
    • Mesibov R., Ordal G. W., Adler J. The range of attractant concentrations for bacterial chemotaxis and the threshold and size of response over this range. Weber law and related phenomena. J. Gen. Physiol. 62:1973;203-223.
    • (1973) J. Gen. Physiol. , vol.62 , pp. 203-223
    • Mesibov, R.1    Ordal, G.W.2    Adler, J.3
  • 30
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science. 268:1995;247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 32
    • 0032492834 scopus 로고    scopus 로고
    • Predicting temporal fluctuations in an intracellular signalling pathway
    • Morton-Firth C. J., Bray D. Predicting temporal fluctuations in an intracellular signalling pathway. J. Theoret. Biol. 192:1998;117-128.
    • (1998) J. Theoret. Biol. , vol.192 , pp. 117-128
    • Morton-Firth, C.J.1    Bray, D.2
  • 33
    • 0023658327 scopus 로고
    • Additive and independent responses in a single receptor: Aspartate and maltose stimuli on the Tar protein
    • Mowbray S. L., Koshland D. E. Additive and independent responses in a single receptor: aspartate and maltose stimuli on the Tar protein. Cell. 50:1987;171-180.
    • (1987) Cell , vol.50 , pp. 171-180
    • Mowbray, S.L.1    Koshland, D.E.2
  • 34
    • 0025150830 scopus 로고
    • Mutations in the aspartate receptor of Escherichi coli which affect aspartate binding
    • Mowbray S. L., Koshland D. E. Mutations in the aspartate receptor of Escherichi coli which affect aspartate binding. J. Biol. Chem. 265:1990;15638-15643.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15638-15643
    • Mowbray, S.L.1    Koshland, D.E.2
  • 35
    • 0029893938 scopus 로고    scopus 로고
    • Modulation of the thermosensing profile of the Escherichia coli aspartate receptor Tar by covalent modification of its methyl-accepting sites
    • Nara T., Kawagishi I., Nishiyama S., Homma M., Imae Y. Modulation of the thermosensing profile of the Escherichia coli aspartate receptor Tar by covalent modification of its methyl-accepting sites. J. Biol. Chem. 271:1996;17932-17936.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17932-17936
    • Nara, T.1    Kawagishi, I.2    Nishiyama, S.3    Homma, M.4    Imae, Y.5
  • 36
    • 0025830353 scopus 로고
    • Reconstitution of the bacterial chemotaxis signal transduction system from purified components
    • Ninfa E. G., Stock A., Mowbray S., Stock J. Reconstitution of the bacterial chemotaxis signal transduction system from purified components. J. Biol. Chem. 266:1991;9764-9770.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9764-9770
    • Ninfa, E.G.1    Stock, A.2    Mowbray, S.3    Stock, J.4
  • 37
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup S. H., Erickson H. P. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc. Natl Acad. Sci. USA. 89:1992;3338-3342.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 38
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson J. S. Signal transduction schemes of bacteria. Cell. 73:1993;857-871.
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 39
    • 0024109926 scopus 로고
    • Receptor interactions through phosphoryaton and methylation pathways in bacterial chemotaxis
    • Sanders D. A., Koshland D. E. Receptor interactions through phosphoryaton and methylation pathways in bacterial chemotaxis. Proc. Natl Acad,. Sci. USA. 85:1988;8425-8429.
    • (1988) Proc. Natl Acad,. Sci. USA , vol.85 , pp. 8425-8429
    • Sanders, D.A.1    Koshland, D.E.2
  • 41
    • 0028928740 scopus 로고
    • Interactions between the methylation sites of the Escherichiacoli aspartate receptor mediated by the methyltransferase
    • Shapiro M. J., Panomitros D., Koshland D. E. Interactions between the methylation sites of the Escherichiacoli aspartate receptor mediated by the methyltransferase. J. Biol. Chem. 270:1995;751-755.
    • (1995) J. Biol. Chem. , vol.270 , pp. 751-755
    • Shapiro, M.J.1    Panomitros, D.2    Koshland, D.E.3
  • 42
    • 0023664532 scopus 로고
    • Purification and characterisation of the S-adenosylmethionine glutamyl methyltransferase that modifies membrane chemoreceptor proteins
    • Simms M. J., Stock A. M., Stock J. B. Purification and characterisation of the S-adenosylmethionine glutamyl methyltransferase that modifies membrane chemoreceptor proteins. J. Biol. Chem. 262:1987;8537-8543.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8537-8543
    • Simms, M.J.1    Stock, A.M.2    Stock, J.B.3
  • 43
    • 0025775705 scopus 로고
    • The kinetic mechanism of S -adenosyl- L -methionine: Glutamylmethyltransferase from Salmonella typhimurium
    • Simms S. A., Subbaramaiah K. The kinetic mechanism of S -adenosyl- L -methionine: glutamylmethyltransferase from Salmonella typhimurium. J. Biol. Chem. 266:1981;12741-12746.
    • (1981) J. Biol. Chem. , vol.266 , pp. 12741-12746
    • Simms, S.A.1    Subbaramaiah, K.2
  • 44
    • 0022405719 scopus 로고
    • Multiple forms of the CheB methylesterase in bacterial chemosensing
    • Simms S. A., Keane M. G., Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J. Biol. Chem. 260:1985;10161-10168.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10161-10168
    • Simms, S.A.1    Keane, M.G.2    Stock, J.3
  • 45
    • 0030739875 scopus 로고    scopus 로고
    • A model of excitation and adaptation in bacterial chemotaxis
    • Spiro P. A., Parkinson J. S., Othmer H. G. A model of excitation and adaptation in bacterial chemotaxis. Proc. Natl Acad. Sci. USA. 94:1996;7263-7268.
    • (1996) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7263-7268
    • Spiro, P.A.1    Parkinson, J.S.2    Othmer, H.G.3
  • 46
    • 0000837558 scopus 로고
    • Quantitation of the sensory response in bacterial chemotaxis
    • Spudich J. L., Koshland D. E. Quantitation of the sensory response in bacterial chemotaxis. Proc. Natl Acad. Sci. USA. 72:1975;710-713.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 710-713
    • Spudich, J.L.1    Koshland, D.E.2
  • 47
    • 0027470710 scopus 로고
    • Activating and inhibitory mutations in the regulatory domain of CheB, the methylesterase in bacterial chemotaxis
    • Stewart R. C. Activating and inhibitory mutations in the regulatory domain of CheB, the methylesterase in bacterial chemotaxis. J. Biol. Chem. 266:1993;1921-1930.
    • (1993) J. Biol. Chem. , vol.266 , pp. 1921-1930
    • Stewart, R.C.1
  • 48
    • 0031042699 scopus 로고    scopus 로고
    • Kinetic characterization of phosphotransfer between CheA and CheY in the bacterial chemotaxis pathway
    • Stewart R. C. Kinetic characterization of phosphotransfer between CheA and CheY in the bacterial chemotaxis pathway. Biochemistry. 36:1997;2030-2040.
    • (1997) Biochemistry , vol.36 , pp. 2030-2040
    • Stewart, R.C.1
  • 49
    • 0019780641 scopus 로고
    • Changing reactivity of receptor carboxyl groups during bacterial sensing
    • Stock J. B., Koshland D. E. Changing reactivity of receptor carboxyl groups during bacterial sensing. J. Biol. Chem. 256:1981;10826-10833.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10826-10833
    • Stock, J.B.1    Koshland, D.E.2
  • 52
    • 0023028640 scopus 로고
    • Kinetics of receptor modification. The multiply methylated aspartate receptors involved in bacterial chemotaxis
    • Terwilliger T. C., Wang J. Y., Koshland D. E. Jr. Kinetics of receptor modification. The multiply methylated aspartate receptors involved in bacterial chemotaxis. J. Biol. Chem. 261:1986;10814-10820.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10814-10820
    • Terwilliger, T.C.1    Wang, J.Y.2    Koshland D.E., Jr.3
  • 53
    • 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., Weis R. M. The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation. Biochemistry. 35:1996;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
  • 54
    • 0030069386 scopus 로고    scopus 로고
    • FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies
    • Zhao R., Amsler C. D., Matsumura P., Shan S. FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies. J. Bacteriol. 178:1996;258-265.
    • (1996) J. Bacteriol. , vol.178 , pp. 258-265
    • Zhao, R.1    Amsler, C.D.2    Matsumura, P.3    Shan, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.