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Volumn 192, Issue 5, 2010, Pages 1193-1200

The chemoreceptor dimer is the unit of conformational coupling and transmembrane signaling

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; LIGAND; NANODISC;

EID: 77749279798     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01391-09     Document Type: Article
Times cited : (34)

References (42)
  • 1
    • 0032444115 scopus 로고    scopus 로고
    • Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: Similar kinase activation but different methyl-accepting activities
    • Barnakov, A., L. Barnakova, and G. Hazelbauer. 1998. Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: similar kinase activation but different methyl-accepting activities. J. Bacteriol. 180: 6713-6718.
    • (1998) J. Bacteriol , vol.180 , pp. 6713-6718
    • Barnakov, A.1    Barnakova, L.2    Hazelbauer, G.3
  • 2
    • 0142179052 scopus 로고    scopus 로고
    • Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers
    • Bayburt, T. H., and S. G. Sligar. 2003. Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers. Protein Sci. 12:2476-2481.
    • (2003) Protein Sci , vol.12 , pp. 2476-2481
    • Bayburt, T.H.1    Sligar, S.G.2
  • 3
    • 50449104169 scopus 로고    scopus 로고
    • Receptor density balances signal stimulation and attenuation in membrane-assembled complexes of bacterial chemotaxis signaling proteins
    • Besschetnova, T. Y., D. J. Montefusco, A. E. Asinas, A. L. Shrout, F. M. Antommattei, and R. M. Weis. 2008. Receptor density balances signal stimulation and attenuation in membrane-assembled complexes of bacterial chemotaxis signaling proteins. Proc. Natl. Acad. Sci. U. S. A. 105:12289-12294.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 12289-12294
    • Besschetnova, T.Y.1    Montefusco, D.J.2    Asinas, A.E.3    Shrout, A.L.4    Antommattei, F.M.5    Weis, R.M.6
  • 4
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog, T., S. Grimme, M. Li, S. G. Sligar, and G. L. Hazelbauer. 2006. Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc. Natl. Acad. Sci. U. S. A. 103:11509-11514.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 5
    • 34250854730 scopus 로고    scopus 로고
    • Using Nanodiscs to create water-soluble transmembrane chemoreceptors inserted in lipid bilayers
    • Boldog, T., M. Li, and G. L. Hazelbauer. 2007. Using Nanodiscs to create water-soluble transmembrane chemoreceptors inserted in lipid bilayers. Methods Enzymol. 423:317-335.
    • (2007) Methods Enzymol , vol.423 , pp. 317-335
    • Boldog, T.1    Li, M.2    Hazelbauer, G.L.3
  • 6
    • 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. U. S. A. 89:6756-6760.
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , pp. 6756-6760
    • Borkovich, K.A.1    Alex, L.A.2    Simon, M.I.3
  • 7
    • 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 J. J. Falke. 2001. Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex. J. Gen. Physiol. 118:693-710.
    • (2001) J. Gen. Physiol , vol.118 , pp. 693-710
    • Bornhorst, J.A.1    Falke, J.J.2
  • 9
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov, I. G., Y. V. Grinkova, A. A. Lazarides, and S. G. Sligar. 2004. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126:3477-3487.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 10
    • 0026031833 scopus 로고    scopus 로고
    • Dunten, P., and D. E. Koshland, Jr. 1991. Tuning the responsiveness of a sensory receptor via covalent modification. J. Biol. Chem. 266:1491-1496.
    • Dunten, P., and D. E. Koshland, Jr. 1991. Tuning the responsiveness of a sensory receptor via covalent modification. J. Biol. Chem. 266:1491-1496.
  • 11
    • 33748364127 scopus 로고    scopus 로고
    • Endres, R. G., and N. S. Wingreen. 2006. Precise adaptation in bacterial chemotaxis through assistance neighborhoods. Proc. Natl. Acad. Sci. U. S. A. 103:13040-13044.
    • Endres, R. G., and N. S. Wingreen. 2006. Precise adaptation in bacterial chemotaxis through "assistance neighborhoods." Proc. Natl. Acad. Sci. U. S. A. 103:13040-13044.
  • 12
    • 0023815085 scopus 로고    scopus 로고
    • Falke, J. J., A. F. Dernburg, D. A. Sternberg, N. Zalkin, D. L. Milligan, and D. E. Koshland, Jr. 1988. Structure of a bacterial sensory receptor. A sitedirected sulfhydryl study. J. Biol. Chem. 263:14850- 14858.
    • Falke, J. J., A. F. Dernburg, D. A. Sternberg, N. Zalkin, D. L. Milligan, and D. E. Koshland, Jr. 1988. Structure of a bacterial sensory receptor. A sitedirected sulfhydryl study. J. Biol. Chem. 263:14850- 14858.
  • 13
    • 0033765068 scopus 로고    scopus 로고
    • Evolutionary conservation of methyl-accepting chemotaxis protein location in bacteria and archaea
    • Gestwicki, J. E., A. C. Lamanna, R. M. Harshey, L. L. McCarter, L. L. Kiessling, and J. Adler. 2000. Evolutionary conservation of methyl-accepting chemotaxis protein location in bacteria and archaea. J. Bacteriol. 182:6499-6502.
    • (2000) J. Bacteriol , vol.182 , pp. 6499-6502
    • Gestwicki, J.E.1    Lamanna, A.C.2    Harshey, R.M.3    McCarter, L.L.4    Kiessling, L.L.5    Adler, J.6
  • 14
    • 67649922591 scopus 로고    scopus 로고
    • Greenfield, D., A. L. McEvoy, H. Shroff, G. E. Crooks, N. S. Wingreen, E. Betzig, and J. Liphardt. 2009. Self-organization of the Escherichia coli chemotaxis network imaged with super-resolution light microscopy. PLoS Biol. 7:e1000137.
    • Greenfield, D., A. L. McEvoy, H. Shroff, G. E. Crooks, N. S. Wingreen, E. Betzig, and J. Liphardt. 2009. Self-organization of the Escherichia coli chemotaxis network imaged with super-resolution light microscopy. PLoS Biol. 7:e1000137.
  • 15
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer, G. L., J. J. Falke, and J. S. Parkinson. 2008. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem. Sci. 33:9-19.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 16
    • 0030959280 scopus 로고    scopus 로고
    • Uncoupling of ligand-binding affinity of the bacterial serine chemoreceptor from methylation- and temperature-modulated signaling states
    • Iwama, T., M. Homma, and I. Kawagishi. 1997. Uncoupling of ligand-binding affinity of the bacterial serine chemoreceptor from methylation- and temperature-modulated signaling states. J. Biol. Chem. 272:13810- 13815.
    • (1997) J. Biol. Chem , vol.272 , pp. 13810-13815
    • Iwama, T.1    Homma, M.2    Kawagishi, I.3
  • 18
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim, K. K., H. Yokota, and S.-H. Kim. 1999. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature 400:787-792.
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.-H.3
  • 19
    • 0018571767 scopus 로고
    • Attractants and repellents influence methylation and demethylation of methyl-accepting chemotaxis proteins in an extract of Escherichia coli
    • Kleene, S. J., A. C. Hobson, and J. Adler. 1979. Attractants and repellents influence methylation and demethylation of methyl-accepting chemotaxis proteins in an extract of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 76:6309-6313.
    • (1979) Proc. Natl. Acad. Sci. U. S. A , vol.76 , pp. 6309-6313
    • Kleene, S.J.1    Hobson, A.C.2    Adler, J.3
  • 20
    • 33746555441 scopus 로고    scopus 로고
    • Adaptational modification and ligand occupancy have opposite effects on positioning of the transmembrane signalling helix of a chemoreceptor
    • Lai, W.-C., B. D. Beel, and G. L. Hazelbauer. 2006. Adaptational modification and ligand occupancy have opposite effects on positioning of the transmembrane signalling helix of a chemoreceptor. Mol. Microbiol. 61:1081-1090.
    • (2006) Mol. Microbiol , vol.61 , pp. 1081-1090
    • Lai, W.-C.1    Beel, B.D.2    Hazelbauer, G.L.3
  • 21
    • 22544472694 scopus 로고    scopus 로고
    • Carboxyl-terminal extensions beyond the conserved pentapeptide reduce rates of chemoreceptor adaptational modification
    • Lai, W.-C., and G. L. Hazelbauer. 2005. Carboxyl-terminal extensions beyond the conserved pentapeptide reduce rates of chemoreceptor adaptational modification. J. Bacteriol. 187:5115-5121.
    • (2005) J. Bacteriol , vol.187 , pp. 5115-5121
    • Lai, W.-C.1    Hazelbauer, G.L.2
  • 22
    • 0032552886 scopus 로고    scopus 로고
    • Le Moual, H., T. Quang, and D. E. Koshland, Jr. 1998. Conformational changes in the cytoplasmic domain of the Escherichia coli aspartate receptor upon adaptive methylation. Biochemistry 37:14852- 14859.
    • Le Moual, H., T. Quang, and D. E. Koshland, Jr. 1998. Conformational changes in the cytoplasmic domain of the Escherichia coli aspartate receptor upon adaptive methylation. Biochemistry 37:14852- 14859.
  • 23
    • 0030736078 scopus 로고    scopus 로고
    • Le Moual, H., T. Quang, and D. E. Koshland, Jr. 1997. Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 36:13441-13448.
    • Le Moual, H., T. Quang, and D. E. Koshland, Jr. 1997. Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 36:13441-13448.
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0030768758 scopus 로고    scopus 로고
    • The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process
    • Li, J., G. Li, and R. M. Weis. 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
  • 27
    • 33645318436 scopus 로고    scopus 로고
    • The carboxyl-terminal linker is important for chemoreceptor function
    • Li, M., and G. L. Hazelbauer. 2006. The carboxyl-terminal linker is important for chemoreceptor function. Mol. Microbiol. 60:469-479.
    • (2006) Mol. Microbiol , vol.60 , pp. 469-479
    • Li, M.1    Hazelbauer, G.L.2
  • 28
    • 2942610579 scopus 로고    scopus 로고
    • Cellular stoichiometry of the components of the chemotaxis signaling complex
    • Li, M., and G. L. Hazelbauer. 2004. Cellular stoichiometry of the components of the chemotaxis signaling complex. J. Bacteriol. 186:3687-3694.
    • (2004) J. Bacteriol , vol.186 , pp. 3687-3694
    • Li, M.1    Hazelbauer, G.L.2
  • 29
    • 0028290945 scopus 로고
    • The serine receptor of bacterial chemotaxis exhibits half-site saturation for serine binding
    • Lin, L. N., J. Li, J. F. Brandts, and R. M. Weis. 1994. The serine receptor of bacterial chemotaxis exhibits half-site saturation for serine binding. Biochemistry 33:6564-6570.
    • (1994) Biochemistry , vol.33 , pp. 6564-6570
    • Lin, L.N.1    Li, J.2    Brandts, J.F.3    Weis, R.M.4
  • 30
    • 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
  • 31
    • 34047215637 scopus 로고    scopus 로고
    • Effects of adaptation in maintaining high sensitivity over a wide range of backgrounds for Escherichia coli chemotaxis
    • Mello, B. A., and Y. Tu. 2007. Effects of adaptation in maintaining high sensitivity over a wide range of backgrounds for Escherichia coli chemotaxis. Biophys. J. 92:2329-2337.
    • (2007) Biophys. J , vol.92 , pp. 2329-2337
    • Mello, B.A.1    Tu, Y.2
  • 32
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M. V., G. G. Prive, D. L. Milligan, W. G. Scott, J. Yeh, J. Jancarik, D. E. Koshland, Jr., and S. H. Kim. 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.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland Jr., D.E.7    Kim, S.H.8
  • 33
    • 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
  • 34
    • 85177008722 scopus 로고    scopus 로고
    • Shapiro, M. J., I. Chakrabarti, and D. E. Koshland, Jr. 1995. Contributions made by individual methylation sites of the Escherichia coli aspartate receptor to chemotactic behavior. Proc. Natl. Acad. Sci. U. S. A. 92:1053-1056.
    • Shapiro, M. J., I. Chakrabarti, and D. E. Koshland, Jr. 1995. Contributions made by individual methylation sites of the Escherichia coli aspartate receptor to chemotactic behavior. Proc. Natl. Acad. Sci. U. S. A. 92:1053-1056.
  • 35
    • 0038399793 scopus 로고    scopus 로고
    • A spatially extended stochastic model of the bacterial chemotaxis signalling pathway
    • Shimizu, T. S., S. V. Aksenov, and D. Bray. 2003. A spatially extended stochastic model of the bacterial chemotaxis signalling pathway. J. Mol. Biol. 329:291-309.
    • (2003) J. Mol. Biol , vol.329 , pp. 291-309
    • Shimizu, T.S.1    Aksenov, S.V.2    Bray, D.3
  • 36
    • 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
  • 37
    • 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. U. S. A. 99:123-127.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 38
    • 1242274351 scopus 로고    scopus 로고
    • Crosslinking snapshots of bacterial chemoreceptor squads
    • Studdert, C. A., and J. S. Parkinson. 2004. Crosslinking snapshots of bacterial chemoreceptor squads. Proc. Natl. Acad. Sci. U. S. A. 101:2117-2122.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 2117-2122
    • Studdert, C.A.1    Parkinson, J.S.2
  • 39
    • 27344455900 scopus 로고    scopus 로고
    • Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies
    • Studdert, C. A., and J. S. Parkinson. 2005. Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies. Proc. Natl. Acad. Sci. U. S. A. 102:15623-15628.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 15623-15628
    • Studdert, C.A.1    Parkinson, J.S.2
  • 40
    • 36848998769 scopus 로고    scopus 로고
    • Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study
    • Swain, K. E., and J. J. Falke. 2007. Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study. Biochemistry 46:13684-13695.
    • (2007) Biochemistry , vol.46 , pp. 13684-13695
    • Swain, K.E.1    Falke, J.J.2
  • 41
    • 33846807515 scopus 로고    scopus 로고
    • Physical responses of bacterial chemoreceptors
    • Vaknin, A., and H. C. Berg. 2007. Physical responses of bacterial chemoreceptors. J. Mol. Biol. 366:1416-1423.
    • (2007) J. Mol. Biol , vol.366 , pp. 1416-1423
    • Vaknin, A.1    Berg, H.C.2
  • 42
    • 34247261989 scopus 로고    scopus 로고
    • Direct visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy
    • Zhang, P., C. M. Khursigara, L. M. Hartnell, and S. Subramaniam. 2007. Direct visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy. Proc. Natl. Acad. Sci. U. S. A. 104:3777-3781.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 3777-3781
    • Zhang, P.1    Khursigara, C.M.2    Hartnell, L.M.3    Subramaniam, S.4


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