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Volumn 1696, Issue 1, 2004, Pages 131-140

Distributed subunit interactions in CheA contribute to dimer stability: A sedimentation equilibrium study

Author keywords

Analytical ultracentrifugation; Association dissociation; Domain interaction; Lipid vesicle

Indexed keywords

CHEA KINASE; DIMER; PROTEIN SUBUNIT;

EID: 1242284199     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.10.001     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe T.W., Stock J.B. The histidine protein kinase superfamily. Adv. Microb. Physiol. 41:1999;139-227.
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 3
    • 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 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, W.4
  • 4
    • 0027521218 scopus 로고
    • Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance
    • Schuster S.C., Swanson R.V., Alex L.A., Bourret R.B., Simon M.I. Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance. Nature. 365:1993;343-347.
    • (1993) Nature , vol.365 , pp. 343-347
    • Schuster, S.C.1    Swanson, R.V.2    Alex, L.A.3    Bourret, R.B.4    Simon, M.I.5
  • 5
    • 0030606898 scopus 로고    scopus 로고
    • Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis
    • LeMoual 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
    • Lemoual, H.1    Koshland Jr., D.E.2
  • 7
    • 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
  • 8
    • 0034622634 scopus 로고    scopus 로고
    • Attractant regulation of the aspartate receptor-kinase complex: Limited cooperative interactions between receptors and effects of the receptor modification state
    • Bornhorst J.A., Falke J.J. Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state. Biochemistry. 39:2000;9486-9493.
    • (2000) Biochemistry , vol.39 , pp. 9486-9493
    • Bornhorst, J.A.1    Falke, J.J.2
  • 9
    • 0037184120 scopus 로고    scopus 로고
    • Receptor methylation controls the magnitude of stimulus-response coupling in bacterial chemotaxis
    • Levit M.N., 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
  • 10
    • 0030043573 scopus 로고    scopus 로고
    • Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
    • Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W. Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry. 35:1996;433-443.
    • (1996) Biochemistry , vol.35 , pp. 433-443
    • Zhou, H.1    McEvoy, M.M.2    Lowry, D.F.3    Swanson, R.V.4    Simon, M.I.5    Dahlquist, F.W.6
  • 11
  • 12
    • 0035903179 scopus 로고    scopus 로고
    • Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
    • Mourey L., Da Re S., Pedelacq J.D., Tolstykh T., Faurie C., Guillet V., Stock J.B., Samama J.P. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem. 276:2001;31074-31082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31074-31082
    • Mourey, L.1    Da Re, S.2    Pedelacq, J.D.3    Tolstykh, T.4    Faurie, C.5    Guillet, V.6    Stock, J.B.7    Samama, J.P.8
  • 13
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell. 96:1999;131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 15
    • 0026023551 scopus 로고
    • Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA
    • Gegner J.A., Dahlquist F.W. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc. Natl. Acad. Sci. U. S. A. 88:1991;750-754.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 750-754
    • Gegner, J.A.1    Dahlquist, F.W.2
  • 16
    • 0027156598 scopus 로고
    • Intermolecular complementation of the kinase activity of CheA
    • Swanson R.V., Bourret R.B., Simon M.I. Intermolecular complementation of the kinase activity of CheA. Mol. Microbiol. 8:1993;435-441.
    • (1993) Mol. Microbiol. , vol.8 , pp. 435-441
    • Swanson, R.V.1    Bourret, R.B.2    Simon, M.I.3
  • 17
    • 0030068603 scopus 로고    scopus 로고
    • Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis
    • Surette M.G., Levit M., Liu Y., Lukat G., Ninfa E.G., Ninfa A., Stock J.B. Dimerization is required for the activity of the protein histidine kinase CheA that mediates signal transduction in bacterial chemotaxis. J. Biol. Chem. 271:1996;939-945.
    • (1996) J. Biol. Chem. , vol.271 , pp. 939-945
    • Surette, M.G.1    Levit, M.2    Liu, Y.3    Lukat, G.4    Ninfa, E.G.5    Ninfa, A.6    Stock, J.B.7
  • 18
    • 0031039355 scopus 로고    scopus 로고
    • Coexpression of the long and short forms of CheA, the chemotaxis histidine kinase, by members of the family Enterobacteriaceae
    • McNamara B.P., Wolfe A.J. Coexpression of the long and short forms of CheA, the chemotaxis histidine kinase, by members of the family Enterobacteriaceae. J. Bacteriol. 179:1997;1813-1818.
    • (1997) J. Bacteriol. , vol.179 , pp. 1813-1818
    • McNamara, B.P.1    Wolfe, A.J.2
  • 19
    • 0026062038 scopus 로고
    • Tandem translation starts in the cheA locus of Escherichia coli
    • Kofoid E.C., Parkinson J.S. Tandem translation starts in the cheA locus of Escherichia coli. J. Bacteriol. 173:1991;2116-2119.
    • (1991) J. Bacteriol. , vol.173 , pp. 2116-2119
    • Kofoid, E.C.1    Parkinson, J.S.2
  • 20
    • 0027467850 scopus 로고
    • The short form of the CheA protein restores kinase activity and chemotactic ability to kinase-deficient mutants
    • Wolfe A.J., Stewart R.C. The short form of the CheA protein restores kinase activity and chemotactic ability to kinase-deficient mutants. Proc. Natl. Acad. Sci. U. S. A. 90:1993;1518-1522.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1518-1522
    • Wolfe, A.J.1    Stewart, R.C.2
  • 21
    • 0031019296 scopus 로고    scopus 로고
    • Phosphorylating and dephosphorylating protein complexes in bacterial chemotaxis
    • Wang H., Matsumara P. Phosphorylating and dephosphorylating protein complexes in bacterial chemotaxis. J. Bacteriol. 179:1997;287-289.
    • (1997) J. Bacteriol. , vol.179 , pp. 287-289
    • Wang, H.1    Matsumara, P.2
  • 22
    • 0029670784 scopus 로고    scopus 로고
    • Characterization of the CheAS/CheZ complex: A specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate
    • Wang H., Matsumura P. Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. Mol. Microbiol. 19:1996;695-703.
    • (1996) Mol. Microbiol. , vol.19 , pp. 695-703
    • Wang, H.1    Matsumura, P.2
  • 23
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik V., 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
  • 25
    • 0029032797 scopus 로고
    • The smaller of two overlapping cheA gene products is not essential for chemotaxis in Escherichia coli
    • Santiania H., Kofoid E.C., Morrison T.B., Parkinson J.S. The smaller of two overlapping cheA gene products is not essential for chemotaxis in Escherichia coli. J. Bacteriol. 177:1995;2713-2720.
    • (1995) J. Bacteriol. , vol.177 , pp. 2713-2720
    • Santiania, H.1    Kofoid, E.C.2    Morrison, T.B.3    Parkinson, J.S.4
  • 26
    • 0029731415 scopus 로고    scopus 로고
    • Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA
    • Levit M., Liu Y., Surette M., Stock J. Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA. J. Biol. Chem. 271:1996;32057-32063.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32057-32063
    • Levit, M.1    Liu, Y.2    Surette, M.3    Stock, J.4
  • 27
    • 1242278865 scopus 로고
    • Overlapping genes at the cheA locus of Escherichia coli
    • Smith R.A., Parkinson J.S. Overlapping genes at the cheA locus of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 88:1980;5370-5374.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5370-5374
    • Smith, R.A.1    Parkinson, J.S.2
  • 28
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier F.W. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:1991;37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 29
    • 0027237735 scopus 로고
    • Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities
    • Swanson R.V., Schuster S.C., Simon M.I. Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities. Biochemistry. 32:1993;7623-7629.
    • (1993) Biochemistry , vol.32 , pp. 7623-7629
    • Swanson, R.V.1    Schuster, S.C.2    Simon, M.I.3
  • 30
    • 0036134273 scopus 로고    scopus 로고
    • Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis
    • Wang W., Malcolm B.A. Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis. Methods Mol. Biol. 182:2002;37-43.
    • (2002) Methods Mol. Biol. , vol.182 , pp. 37-43
    • Wang, W.1    Malcolm, B.A.2
  • 32
    • 0027231876 scopus 로고
    • Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis
    • Bray D., Bourret R.B., Simon M.I. Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis. Mol. Biol. Cell. 4:1993;469-482.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 469-482
    • Bray, D.1    Bourret, R.B.2    Simon, M.I.3
  • 33
    • 0034119460 scopus 로고    scopus 로고
    • Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli
    • Boesch K.C., Silversmith R.E., Bourret R.B. Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli. J. Bacteriol. 182:2000;3544-3552.
    • (2000) J. Bacteriol. , vol.182 , pp. 3544-3552
    • Boesch, K.C.1    Silversmith, R.E.2    Bourret, R.B.3
  • 34
    • 0026345261 scopus 로고
    • Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli
    • Hess J.F., Bourret R.B., Simon M.I. Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli. Meth. Enzymol. 200:1991;188-204.
    • (1991) Meth. Enzymol. , vol.200 , pp. 188-204
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 35
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 37
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson M.L., Correia J.J., Yphantis D.A., Halvorson H.R. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:1981;575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 38
    • 0033580642 scopus 로고    scopus 로고
    • Mechanism of CheA protein kinase activation in receptor signaling complexes
    • Levit M.N., Liu Y., Stock J.B. Mechanism of CheA protein kinase activation in receptor signaling complexes. Biochemistry. 38:1999;6651-6658.
    • (1999) Biochemistry , vol.38 , pp. 6651-6658
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 39
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants tris(2-carboxyethyl) phosphine and dithiothreitol for use in protein biochemistry
    • Getz E.B., Xiao M., Chakrabarty T., Cooke R., Selvin P.R. A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry. Anal. Biochem. 273:1999;73-80.
    • (1999) Anal. Biochem. , vol.273 , pp. 73-80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 40
    • 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
  • 41
    • 0036312369 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ
    • Zhao R., Collins E.J., Bourret R.B., Silversmith R.E. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nat. Struct. Biol. 9:2002;570-575.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 570-575
    • Zhao, R.1    Collins, E.J.2    Bourret, R.B.3    Silversmith, R.E.4
  • 42
    • 0034728565 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a high-affinity trivalent system derived from vancomycin and L-Lys-D-Ala-D-Ala
    • Rao J.H., Lahiri J., Weis R.M., Whitesides G.M. Design, synthesis, and characterization of a high-affinity trivalent system derived from vancomycin and L-Lys-D-Ala-D-Ala. J. Am. Chem. Soc. 122:2000;2698-2710.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2698-2710
    • Rao, J.H.1    Lahiri, J.2    Weis, R.M.3    Whitesides, G.M.4
  • 43
    • 0034870959 scopus 로고    scopus 로고
    • Contribution of translational and rotational motions to molecular association in aqueous solution
    • Yu Y.B., Privalov P.L., Hodges R.S. Contribution of translational and rotational motions to molecular association in aqueous solution. Biophys. J. 81:2001;1632-1642.
    • (2001) Biophys. J. , vol.81 , pp. 1632-1642
    • Yu, Y.B.1    Privalov, P.L.2    Hodges, R.S.3
  • 44
    • 0036681414 scopus 로고    scopus 로고
    • Entropic benefit of a cross-link in protein association
    • Zaman M.H., Berry R.S., Sosnick T.R. Entropic benefit of a cross-link in protein association. Proteins. 48:2002;341-351.
    • (2002) Proteins , vol.48 , pp. 341-351
    • Zaman, M.H.1    Berry, R.S.2    Sosnick, T.R.3
  • 45
    • 0036677555 scopus 로고    scopus 로고
    • On the calculation of absolute macromolecular binding free energies
    • Luo H., Sharp K. On the calculation of absolute macromolecular binding free energies. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10399-10404.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10399-10404
    • Luo, H.1    Sharp, K.2
  • 47
    • 0036220793 scopus 로고    scopus 로고
    • Binding and diffusion of CheR molecules within a cluster of membrane receptors
    • Levin M.D., Shimizu T.S., Bray D. Binding and diffusion of CheR molecules within a cluster of membrane receptors. Biophys. J. 82:2002;1809-1817.
    • (2002) Biophys. J. , vol.82 , pp. 1809-1817
    • Levin, M.D.1    Shimizu, T.S.2    Bray, D.3
  • 48
    • 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
  • 49
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren A., Eisenbach M. How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182:2000;6865-6873.
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 50
    • 0028869205 scopus 로고
    • The response regulators CheB and CheY exhibit competitive binding to the kinase CheA
    • Li J., Swanson R.V., Simon M.I., Weis R.M. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry. 34:1995;14626-14636.
    • (1995) Biochemistry , vol.34 , pp. 14626-14636
    • Li, J.1    Swanson, R.V.2    Simon, M.I.3    Weis, R.M.4


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