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Volumn 366, Issue 5, 2007, Pages 1416-1423

Physical Responses of Bacterial Chemoreceptors

Author keywords

chemotaxis; fluorescence polarization; fluorescence resonance energy transfer; membrane proteins; receptors

Indexed keywords

BACTERIAL PROTEIN; DIMER; OLIGOMER; PHOSPHOTRANSFERASE; POLYMER;

EID: 33846807515     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.12.024     Document Type: Article
Times cited : (85)

References (43)
  • 1
    • 0032968708 scopus 로고    scopus 로고
    • The dynamics of T cell receptor signaling: complex orchestration and the key roles of tempo and cooperation
    • Germain R.N., and Stefanova I. The dynamics of T cell receptor signaling: complex orchestration and the key roles of tempo and cooperation. Annu. Rev. Immunol. 17 (1999) 467-522
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 467-522
    • Germain, R.N.1    Stefanova, I.2
  • 2
    • 0042467972 scopus 로고    scopus 로고
    • Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons
    • Agnati L.F., Ferre S., Lluis C., Franco R., and Fuxe K. Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons. Pharmacol. Rev. 55 (2003) 509-550
    • (2003) Pharmacol. Rev. , vol.55 , pp. 509-550
    • Agnati, L.F.1    Ferre, S.2    Lluis, C.3    Franco, R.4    Fuxe, K.5
  • 3
    • 3042651100 scopus 로고    scopus 로고
    • Conformational spread: the propagation of allosteric states in large multiprotein complexes
    • Bray D., and Duke T. Conformational spread: the propagation of allosteric states in large multiprotein complexes. Annu. Rev. Biophys. Biomol. Structure 33 (2004) 53-73
    • (2004) Annu. Rev. Biophys. Biomol. Structure , vol.33 , pp. 53-73
    • Bray, D.1    Duke, T.2
  • 4
    • 0023917333 scopus 로고
    • Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis
    • Milligan D.L., and Koshland Jr. D.E. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J. Biol. Chem. 263 (1988) 6268-6275
    • (1988) J. Biol. Chem. , vol.263 , pp. 6268-6275
    • Milligan, D.L.1    Koshland Jr., D.E.2
  • 5
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim K.K., Yokota H., and 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
  • 7
    • 1242274351 scopus 로고    scopus 로고
    • Crosslinking snapshots of bacterial chemoreceptor squads
    • Studdert C.A., and Parkinson J.S. Crosslinking snapshots of bacterial chemoreceptor squads. Proc. Natl Acad. Sci. USA 101 (2004) 2117-2122
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2117-2122
    • Studdert, C.A.1    Parkinson, J.S.2
  • 9
    • 33745172449 scopus 로고    scopus 로고
    • Conformational suppression of inter-receptor signaling defects
    • Ames P., and Parkinson J.S. Conformational suppression of inter-receptor signaling defects. Proc. Natl Acad. Sci. USA 103 (2006) 9292-9297
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9292-9297
    • Ames, P.1    Parkinson, J.S.2
  • 10
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik V., and Berg H.C. Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 37 (2000) 740-751
    • (2000) Mol. Microbiol. , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 11
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock J.R., and 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
  • 12
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray D., Levin M.D., and 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
    • 7944221332 scopus 로고    scopus 로고
    • Receptor clustering and signal processing in E. coli chemotaxis
    • Sourjik V. Receptor clustering and signal processing in E. coli chemotaxis. Trends Microbiol. 12 (2004) 569-576
    • (2004) Trends Microbiol. , vol.12 , pp. 569-576
    • Sourjik, V.1
  • 14
    • 0034603209 scopus 로고    scopus 로고
    • Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli
    • Li G., and 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
  • 15
    • 0037184120 scopus 로고    scopus 로고
    • Receptor methylation controls the magnitude of stimulus-response coupling in bacterial chemotaxis
    • Levit M.N., and Stock J.B. Receptor methylation controls the magnitude of stimulus-response coupling in bacterial chemotaxis. J. Biol. Chem. 277 (2002) 36760-36765
    • (2002) J. Biol. Chem. , vol.277 , pp. 36760-36765
    • Levit, M.N.1    Stock, J.B.2
  • 16
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik V., and Berg H.C. Receptor sensitivity in bacterial chemotaxis. Proc. Natl Acad. Sci. USA 99 (2002) 123-127
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 17
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik V., and Berg H.C. Functional interactions between receptors in bacterial chemotaxis. Nature 428 (2004) 437-441
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 18
    • 0000540586 scopus 로고    scopus 로고
    • Cooperative model of bacterial sensing
    • Shi Y., and Duke T. Cooperative model of bacterial sensing. Phys. Rev. E 58 (1998) 6399
    • (1998) Phys. Rev. E , vol.58 , pp. 6399
    • Shi, Y.1    Duke, T.2
  • 19
    • 0033621154 scopus 로고    scopus 로고
    • Heightened sensitivity of a lattice of membrane receptors
    • Duke T.A.J., and Bray D. Heightened sensitivity of a lattice of membrane receptors. Proc. Natl Acad. Sci. USA 96 (1999) 10104-10108
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10104-10108
    • Duke, T.A.J.1    Bray, D.2
  • 20
    • 0037816259 scopus 로고    scopus 로고
    • Quantitative modeling of sensitivity in bacterial chemotaxis: the role of coupling among different chemoreceptor species
    • Mello B.A., and Tu Y. Quantitative modeling of sensitivity in bacterial chemotaxis: the role of coupling among different chemoreceptor species. Proc. Natl Acad. Sci. USA 100 (2003) 8223-8228
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8223-8228
    • Mello, B.A.1    Tu, Y.2
  • 21
    • 0038399793 scopus 로고    scopus 로고
    • A spatially extended stochastic model of the bacterial chemotaxis signalling pathway
    • Shimizu T.S., Aksenov S.V., and Bray D. A spatially extended stochastic model of the bacterial chemotaxis signalling pathway. J. Mol. Biol. 329 (2003) 291-309
    • (2003) J. Mol. Biol. , vol.329 , pp. 291-309
    • Shimizu, T.S.1    Aksenov, S.V.2    Bray, D.3
  • 22
    • 2142753979 scopus 로고    scopus 로고
    • Dynamic receptor team formation can explain the high signal transduction gain in Escherichia coli
    • Albert R., Chiu Y.-w., and Othmer H.G. Dynamic receptor team formation can explain the high signal transduction gain in Escherichia coli. Biophys. J. 86 (2004) 2650-2659
    • (2004) Biophys. J. , vol.86 , pp. 2650-2659
    • Albert, R.1    Chiu, Y.-w.2    Othmer, H.G.3
  • 23
    • 4444270835 scopus 로고    scopus 로고
    • Effects of receptor interaction in bacterial chemotaxis
    • Mello B.A., Shaw L., and Tu Y. Effects of receptor interaction in bacterial chemotaxis. Biophys. J. 87 (2004) 1578-1595
    • (2004) Biophys. J. , vol.87 , pp. 1578-1595
    • Mello, B.A.1    Shaw, L.2    Tu, Y.3
  • 24
    • 4644278216 scopus 로고    scopus 로고
    • An allosteric model for transmembrane signaling in bacterial chemotaxis
    • Rao C.V., Frenklach M., and Arkin A.P. An allosteric model for transmembrane signaling in bacterial chemotaxis. J. Mol. Biol. 343 (2004) 291-303
    • (2004) J. Mol. Biol. , vol.343 , pp. 291-303
    • Rao, C.V.1    Frenklach, M.2    Arkin, A.P.3
  • 25
    • 28444449791 scopus 로고    scopus 로고
    • An allosteric model for heterogeneous receptor complexes: understanding bacterial chemotaxis responses to multiple stimuli
    • Mello B.A., and Tu Y. An allosteric model for heterogeneous receptor complexes: understanding bacterial chemotaxis responses to multiple stimuli. Proc. Natl Acad. Sci. USA 102 (2005) 17354-17359
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17354-17359
    • Mello, B.A.1    Tu, Y.2
  • 27
    • 33744798728 scopus 로고    scopus 로고
    • Receptor-receptor coupling in bacterial chemotaxis: evidence for strongly coupled clusters
    • Skoge M.L., Endres R.G., and Wingreen N.S. Receptor-receptor coupling in bacterial chemotaxis: evidence for strongly coupled clusters. Biophys. J. 90 (2006) 4317-4326
    • (2006) Biophys. J. , vol.90 , pp. 4317-4326
    • Skoge, M.L.1    Endres, R.G.2    Wingreen, N.S.3
  • 28
    • 31444435736 scopus 로고    scopus 로고
    • Osmotic stress mechanically perturbs chemoreceptors in Escherichia coli
    • Vaknin A., and Berg H.C. Osmotic stress mechanically perturbs chemoreceptors in Escherichia coli. Proc. Natl Acad. Sci. USA 103 (2006) 592-596
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 592-596
    • Vaknin, A.1    Berg, H.C.2
  • 29
    • 0035195796 scopus 로고    scopus 로고
    • Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex
    • Bornhorst J.A., and Falke J.J. Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex. J. Gen. Physiol. 118 (2001) 639-710
    • (2001) J. Gen. Physiol. , vol.118 , pp. 639-710
    • Bornhorst, J.A.1    Falke, J.J.2
  • 30
    • 0021724874 scopus 로고
    • Two-state model for bacterial chemoreceptor proteins: the role of multiple methylation
    • Asakura S., and 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
  • 31
    • 0030797355 scopus 로고    scopus 로고
    • Robustness in simple biochemical networks
    • Barkai N., and 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
  • 32
    • 0028878506 scopus 로고
    • Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12
    • Pina K., Navarro C., McWalter L., Boxer D.H., Price N.C., Kelly S.M., et al. Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12. Eur. J. Biochem. 227 (1995) 857-865
    • (1995) Eur. J. Biochem. , vol.227 , pp. 857-865
    • Pina, K.1    Navarro, C.2    McWalter, L.3    Boxer, D.H.4    Price, N.C.5    Kelly, S.M.6
  • 33
    • 13444283382 scopus 로고    scopus 로고
    • Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor
    • Draheim R.R., Bormans A.F., Lai R.-Z., and Manson M.D. Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor. Biochemistry 44 (2005) 1268-1277
    • (2005) Biochemistry , vol.44 , pp. 1268-1277
    • Draheim, R.R.1    Bormans, A.F.2    Lai, R.-Z.3    Manson, M.D.4
  • 34
    • 20344372661 scopus 로고    scopus 로고
    • Adaptational assistance in clusters of bacterial chemoreceptors
    • Mingshan L., and Hazelbauer G.L. Adaptational assistance in clusters of bacterial chemoreceptors. Mol. Microbiol. 56 (2005) 1617-1626
    • (2005) Mol. Microbiol. , vol.56 , pp. 1617-1626
    • Mingshan, L.1    Hazelbauer, G.L.2
  • 35
    • 7744226148 scopus 로고    scopus 로고
    • Ligand-specific activation of Escherichia coli chemoreceptor transmethylation
    • Antommattei F.M., Munzner J.B., and Weis R.M. Ligand-specific activation of Escherichia coli chemoreceptor transmethylation. J. Bacteriol. 186 (2004) 7556-7563
    • (2004) J. Bacteriol. , vol.186 , pp. 7556-7563
    • Antommattei, F.M.1    Munzner, J.B.2    Weis, R.M.3
  • 36
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke J.J., and 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
  • 37
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko M., Berndt F., Gruber M., Linder J.U., Truffault V., Schultz A., et al. The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126 (2006) 929-940
    • (2006) Cell , vol.126 , pp. 929-940
    • Hulko, M.1    Berndt, F.2    Gruber, M.3    Linder, J.U.4    Truffault, V.5    Schultz, A.6
  • 39
    • 1242352964 scopus 로고    scopus 로고
    • Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor
    • Miller A.S., and Falke J.J. Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor. Biochemistry 43 (2004) 1763-1770
    • (2004) Biochemistry , vol.43 , pp. 1763-1770
    • Miller, A.S.1    Falke, J.J.2
  • 40
    • 33747673594 scopus 로고    scopus 로고
    • Control of chemotactic signal gain via modulation of a pre-formed receptor array
    • Irieda H., Homma M., Homma M., and Kawagishi I. Control of chemotactic signal gain via modulation of a pre-formed receptor array. J. Biol. Chem. 281 (2006) 23880-23886
    • (2006) J. Biol. Chem. , vol.281 , pp. 23880-23886
    • Irieda, H.1    Homma, M.2    Homma, M.3    Kawagishi, I.4
  • 41
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog T., Grimme S., Li M., Sligar S.G., and Hazelbauer G.L. Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc. Natl Acad. Sci. USA 103 (2006) 11509-11514
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 42
    • 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., and 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
  • 43
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., Violin J.D., Newton A.C., and Tsien R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296 (2002) 913-916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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