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Volumn 48, Issue 27, 2009, Pages 6412-6422

The two active sites of thermotoga maritima CheA dimers bind ATP with dramatically different affinities

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ATP-BINDING SITE; AUTOPHOSPHORYLATION; BACTERIAL CELLS; CENTRAL COMPONENT; DIMERIC PROTEINS; ENVIRONMENTAL CUES; HIGH-AFFINITY SITES; HISTIDINE KINASE; HOMODIMERS; NUCLEOTIDE ANALOGUES; PHOSPHORYL GROUPS; PHOSPHORYLATION REACTIONS; PROKARYOTIC CELLS; SIDE CHAINS; SIGNAL TRANSDUCTION PATHWAYS; SINGLE SITES; THERMOTOGA MARITIMA; TRIPHOSPHATE;

EID: 67650079187     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900474g     Document Type: Article
Times cited : (13)

References (66)
  • 1
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A., Alex, L., Crane, B. R., and Simon, M. I. (1999) Structure of CheA, a signal-transducing histidine kinase. Cell 96, 131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.1    Alex, L.2    Crane, B.R.3    Simon, M.I.4
  • 4
    • 0025647599 scopus 로고
    • The dynamics of protein phosphorylation in bacterial chemotaxis
    • Borkovich, K. A., and Simon, M. I. (1990) The dynamics of protein phosphorylation in bacterial chemotaxis. Cell 63, 1339-1348.
    • (1990) Cell , vol.63 , pp. 1339-1348
    • Borkovich, K.A.1    Simon, M.I.2
  • 5
    • 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., and Falke, J. J. (2000) Attractant regulation of the aspartate receptor-kinase complex: Limited cooperative interactions between receptors and effects of the receptor modification state. Biochemistry 39, 9486-9493.
    • (2000) Biochemistry , vol.39 , pp. 9486-9493
    • Bornhorst, J.A.1    Falke, J.J.2
  • 6
    • 0027502587 scopus 로고
    • The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW
    • Bourret, R. B., Davagnino, J., and Simon, M. I. (1993) The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW. J. Bacteriol. 175, 2097-2101.
    • (1993) J. Bacteriol , vol.175 , pp. 2097-2101
    • Bourret, R.B.1    Davagnino, J.2    Simon, M.I.3
  • 7
    • 29344461522 scopus 로고    scopus 로고
    • Breaking symmetry in protein dimers: Designs and functions
    • Brown, J. H. (2006) Breaking symmetry in protein dimers: Designs and functions. Protein Sci. 15, 1-13.
    • (2006) Protein Sci , vol.15 , pp. 1-13
    • Brown, J.H.1
  • 8
    • 67650050633 scopus 로고    scopus 로고
    • Creighton, T. C. (1993) Proteins. Structures and Molecular Properties , 2nd ed., pp 381-382, W. H. Freeman and Co., New York.
    • Creighton, T. C. (1993) Proteins. Structures and Molecular Properties , 2nd ed., pp 381-382, W. H. Freeman and Co., New York.
  • 9
    • 34047271417 scopus 로고    scopus 로고
    • Modeling and numerical simulation of biotin carboxylase kinetics: Implications for half-sites reactivity
    • DeQueiroz, M. S., and Waldrop, G. L. (2007) Modeling and numerical simulation of biotin carboxylase kinetics: Implications for half-sites reactivity. J. Theor. Biol. 246, 167-175.
    • (2007) J. Theor. Biol , vol.246 , pp. 167-175
    • DeQueiroz, M.S.1    Waldrop, G.L.2
  • 10
    • 67650062371 scopus 로고    scopus 로고
    • Ph.D. Thesis, University of Maryland, College Park, MD
    • Eaton, A. K. (2008) Ph.D. Thesis, University of Maryland, College Park, MD.
    • (2008)
    • Eaton, A.K.1
  • 12
    • 0026023551 scopus 로고
    • Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA
    • Gegner, J., and Dahlquist, F. W. (1991) Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc. Natl. Acad. Sci. U.S.A. 88, 750-754.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 750-754
    • Gegner, J.1    Dahlquist, F.W.2
  • 13
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert, S. P., Moyer, M. L., and Johnson, K. A. (1998) Alternating site mechanism of the kinesin ATPase. Biochemistry 37, 792-799.
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 14
    • 65449157697 scopus 로고    scopus 로고
    • Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation
    • Gloor, S. L., and Falke, J. J. (2009) Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation. Biochemistry 48, 3631-3644.
    • (2009) Biochemistry , vol.48 , pp. 3631-3644
    • Gloor, S.L.1    Falke, J.J.2
  • 15
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe, T. W., and Stock, J. B. (1999) The histidine protein kinase superfamily. Adv. Microb. Physiol. 41, 139-227.
    • (1999) Adv. Microb. Physiol , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 16
    • 0020491305 scopus 로고    scopus 로고
    • Gresser, M. J., Myers, J. A., and Boyer, P. D. (1982) ) Catalytic site cooperativity of beef-heart mitochondrial F, adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three site model. J. Biol. Chem. 257, 12030-12038.
    • Gresser, M. J., Myers, J. A., and Boyer, P. D. (1982) ) Catalytic site cooperativity of beef-heart mitochondrial F, adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three site model. J. Biol. Chem. 257, 12030-12038.
  • 17
    • 0023723766 scopus 로고
    • Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis
    • Hess, J. F., Bourret, R. B., and Simon, M. I. (1988) Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 336, 139-143.
    • (1988) Nature , vol.336 , pp. 139-143
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 18
    • 0026345261 scopus 로고
    • Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli
    • Hess, J. F., Bourret, R. B., and Simon, M. I. (1991) Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli. Methods Enzymol. 200, 188-204.
    • (1991) Methods Enzymol , vol.200 , pp. 188-204
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 19
    • 0041323078 scopus 로고    scopus 로고
    • Fluorescent and colored trinitrophenylated analogs of ATP and GTP
    • Hiratsuka, T. (2003) Fluorescent and colored trinitrophenylated analogs of ATP and GTP. Eur. J. Biochem. 270, 3479-3485.
    • (2003) Eur. J. Biochem , vol.270 , pp. 3479-3485
    • Hiratsuka, T.1
  • 20
    • 0015894660 scopus 로고
    • Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine-5′- triphosphate, an analog of adenosine triphosphate
    • Hiratsuka, T., and Uchida, K. (1973) Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine-5′- triphosphate, an analog of adenosine triphosphate. Biochim. Biophys. Acta 320, 635-647.
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 635-647
    • Hiratsuka, T.1    Uchida, K.2
  • 21
    • 67650025049 scopus 로고    scopus 로고
    • Ph.D. Thesis, University of Maryland, College Park, MD
    • Hirschman, A. (2002) Ph.D. Thesis, University of Maryland, College Park, MD.
    • (2002)
    • Hirschman, A.1
  • 22
    • 0035923402 scopus 로고    scopus 로고
    • Active site mutations in CheA, the signal-transducing protein kinase of the chemotaxis system in Escherichia coli
    • Hirschman, A., Boukhvalova, M., VanBruggen, R., Wolfe, A. J., and Stewart, R. C. (2001) Active site mutations in CheA, the signal-transducing protein kinase of the chemotaxis system in Escherichia coli. Biochemistry 40, 13876-13887.
    • (2001) Biochemistry , vol.40 , pp. 13876-13887
    • Hirschman, A.1    Boukhvalova, M.2    VanBruggen, R.3    Wolfe, A.J.4    Stewart, R.C.5
  • 23
    • 0026055806 scopus 로고
    • Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies
    • Hoffman, A., and Roeder, R. G. (1991) Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies. Nucleic Acids Res. 19, 6337-6338.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6337-6338
    • Hoffman, A.1    Roeder, R.G.2
  • 24
    • 0034595228 scopus 로고    scopus 로고
    • Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein Nitrogen Regulator II
    • Jiang, P., Peliska, J. S., and Ninfa, A. J. (2000) Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein Nitrogen Regulator II. Biochemistry 39, 5057-5065.
    • (2000) Biochemistry , vol.39 , pp. 5057-5065
    • Jiang, P.1    Peliska, J.S.2    Ninfa, A.J.3
  • 25
    • 1242284199 scopus 로고    scopus 로고
    • Distributed subunit interactions in CheA contribute to dimer stability: A sedimentation equilibrium study
    • Kott, L., Braswell, E. H., Shrout, A. L., and Weis, R. M. (2004) Distributed subunit interactions in CheA contribute to dimer stability: A sedimentation equilibrium study. Biochim. Biophys. Acta 1696, 131-140.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 131-140
    • Kott, L.1    Braswell, E.H.2    Shrout, A.L.3    Weis, R.M.4
  • 26
    • 0032573506 scopus 로고    scopus 로고
    • Cooperativity and flexibility of active sites in homodimeric transketolase
    • Kovina, M. V., and Kochetov, G. A. (1998) Cooperativity and flexibility of active sites in homodimeric transketolase. FEBS Lett. 440, 81-84.
    • (1998) FEBS Lett , vol.440 , pp. 81-84
    • Kovina, M.V.1    Kochetov, G.A.2
  • 27
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase. Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 30
    • 0029731415 scopus 로고    scopus 로고
    • Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA
    • Levit, M., Liu, Y., Surette, M., and Stock, J. (1996) Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA. J. Biol. Chem. 271, 32057-32063.
    • (1996) J. Biol. Chem , vol.271 , pp. 32057-32063
    • Levit, M.1    Liu, Y.2    Surette, M.3    Stock, J.4
  • 31
    • 0028869205 scopus 로고
    • The response regulators CheB and CheY exhibit competitive binding to the kinase CheA
    • Li, J., Swanson, R. V., Simon, M. I., and Weis, R. M. (1995) The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry 34, 14626-1463.
    • (1995) Biochemistry , vol.34 , pp. 14626-21463
    • Li, J.1    Swanson, R.V.2    Simon, M.I.3    Weis, R.M.4
  • 32
    • 0024347198 scopus 로고
    • Phosphorylation of an N-terminal regulatory domain activates the methylesterase in bacterial chemotaxis
    • Lupas, A., and Stock, J. B. (1989) Phosphorylation of an N-terminal regulatory domain activates the methylesterase in bacterial chemotaxis. J. Biol. Chem. 264, 17337-17342.
    • (1989) J. Biol. Chem , vol.264 , pp. 17337-17342
    • Lupas, A.1    Stock, J.B.2
  • 33
    • 0032560570 scopus 로고    scopus 로고
    • Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway
    • McEvoy, M. M., Hausrath, A. C., Randolph, G. B., Remington, S. J., and Dahlquist, F. W. (1998) Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc. Natl. Acad. Sci. U.S.A. 95, 7333-7338.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 7333-7338
    • McEvoy, M.M.1    Hausrath, A.C.2    Randolph, G.B.3    Remington, S.J.4    Dahlquist, F.W.5
  • 34
    • 0029931125 scopus 로고    scopus 로고
    • Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy
    • McEvoy, M. M., Muhandiram, D. R., Kay, L. E., and Dahlquist, F. W. (1996) Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry 35, 5633-5640.
    • (1996) Biochemistry , vol.35 , pp. 5633-5640
    • McEvoy, M.M.1    Muhandiram, D.R.2    Kay, L.E.3    Dahlquist, F.W.4
  • 35
    • 0028851794 scopus 로고
    • Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli
    • McEvoy, M. M., Zhou, J., Roth, A. F., Lowry, D. F., Morrison, T. B., Kay, L. E., and Dahlquist, F. W. (1995) Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry 34, 13871-13880.
    • (1995) Biochemistry , vol.34 , pp. 13871-13880
    • McEvoy, M.M.1    Zhou, J.2    Roth, A.F.3    Lowry, D.F.4    Morrison, T.B.5    Kay, L.E.6    Dahlquist, F.W.7
  • 36
    • 0025897515 scopus 로고
    • Communication between the active sites in dimeric mercuric ion reductase: An alternating sites hypothesis for catalysis
    • Miller, S. M., Massey, V., Williams, C. H.Jr., Ballou, D. P., and Walsh, C. T. (1991) Communication between the active sites in dimeric mercuric ion reductase: An alternating sites hypothesis for catalysis. Biochemistry 30, 2600-2612.
    • (1991) Biochemistry , vol.30 , pp. 2600-2612
    • Miller, S.M.1    Massey, V.2    Williams Jr., C.H.3    Ballou, D.P.4    Walsh, C.T.5
  • 37
    • 0028240995 scopus 로고
    • Liberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli
    • Morrison, T. B., and Parkinson, J. S. (1994) Liberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 91, 5485-5489.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 5485-5489
    • Morrison, T.B.1    Parkinson, J.S.2
  • 38
    • 0030886624 scopus 로고    scopus 로고
    • A fragment liberated from the E. coli kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling
    • Morrison, T. B., and Parkinson, J. S. (1997) A fragment liberated from the E. coli kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling. J. Bacteriol. 179, 5543-5550.
    • (1997) J. Bacteriol , vol.179 , pp. 5543-5550
    • Morrison, T.B.1    Parkinson, J.S.2
  • 39
    • 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., and Samama, J.-P. (2001) Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem. 276, 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
  • 40
    • 0035808273 scopus 로고    scopus 로고
    • Interdomain interactions in oligomeric enzymes: Creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers
    • Nagradova, N. K. (2001) Interdomain interactions in oligomeric enzymes: Creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers. FEBS Lett. 487, 327-332.
    • (2001) FEBS Lett , vol.487 , pp. 327-332
    • Nagradova, N.K.1
  • 41
    • 0001015633 scopus 로고
    • Neidhardt, F. C, Ingraham, J. L, Low, K. B, Magasanik, B, Schaechter, M, and Umbarger, H. E, Eds, pp, ASM Press, Washington, DC
    • Neuhard, J., and Nygaard, P. (1987) in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger, H. E., Eds.) pp 445-473, ASM Press, Washington, DC.
    • (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 445-473
    • Neuhard, J.1    Nygaard, P.2
  • 42
    • 0027439298 scopus 로고
    • Mechanism of autophosphorylation of Escherichia coli Nitrogen Regulator II (NRII or NtrB): Trans-phosphorylation between subunits
    • Ninfa, E. G., Atkinson, M. R., Kamberov, E. S., and Ninfa, A. J. (1993) Mechanism of autophosphorylation of Escherichia coli Nitrogen Regulator II (NRII or NtrB): trans-phosphorylation between subunits. J. Bacteriol. 175, 7024-7032.
    • (1993) J. Bacteriol , vol.175 , pp. 7024-7032
    • Ninfa, E.G.1    Atkinson, M.R.2    Kamberov, E.S.3    Ninfa, A.J.4
  • 43
    • 4143085007 scopus 로고    scopus 로고
    • In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved
    • Park, S.-Y., Beel, B. D., Simon, M. I., Bilwes, A. M., and Crane, B. R. (2004) In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved. Proc. Natl. Acad. Sci. U.S.A. 101, 11646-11651.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 11646-11651
    • Park, S.-Y.1    Beel, B.D.2    Simon, M.I.3    Bilwes, A.M.4    Crane, B.R.5
  • 45
    • 1442300985 scopus 로고    scopus 로고
    • Subunit exchange by CheA histidine kinases from mesophile Escherichia coli and the thermophile Thermotoga maritima
    • Park, S.-Y., Quezada, C. M., Bilwes, A. M., and Crane, B. R. (2004) Subunit exchange by CheA histidine kinases from mesophile Escherichia coli and the thermophile Thermotoga maritima. Biochemistry 43, 2228-2240.
    • (2004) Biochemistry , vol.43 , pp. 2228-2240
    • Park, S.-Y.1    Quezada, C.M.2    Bilwes, A.M.3    Crane, B.R.4
  • 47
    • 4143077357 scopus 로고    scopus 로고
    • Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima
    • Quezada, C. M., Gradinaru, C., Simon, M. I., Bilwes, A. M., and Crane, B. R. (2004) Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima. J. Mol. Biol. 341, 1283-1294.
    • (2004) J. Mol. Biol , vol.341 , pp. 1283-1294
    • Quezada, C.M.1    Gradinaru, C.2    Simon, M.I.3    Bilwes, A.M.4    Crane, B.R.5
  • 48
    • 24044550283 scopus 로고    scopus 로고
    • Structural and chemical requirements for histidine phosphorylation by the chemotaxis kinase CheA
    • Quezada, C. M., Hamel, D. J., Gradinaru, C., Bilwes, A. M., Dahlquist, F. W., Crane, B. R., and Simon, M. I. (2005) Structural and chemical requirements for histidine phosphorylation by the chemotaxis kinase CheA. J. Biol. Chem. 280, 39581-30585.
    • (2005) J. Biol. Chem , vol.280 , pp. 39581-30585
    • Quezada, C.M.1    Hamel, D.J.2    Gradinaru, C.3    Bilwes, A.M.4    Dahlquist, F.W.5    Crane, B.R.6    Simon, M.I.7
  • 49
    • 1542319732 scopus 로고    scopus 로고
    • Relationship between growth rate and ATP concentration in Escherichia coli: A bioassay for available cellular ATP
    • Schneider, D. A., and Gourse, R. L. (2004) Relationship between growth rate and ATP concentration in Escherichia coli: A bioassay for available cellular ATP. J. Biol. Chem. 279, 8262-8268.
    • (2004) J. Biol. Chem , vol.279 , pp. 8262-8268
    • Schneider, D.A.1    Gourse, R.L.2
  • 50
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V., and Berg, H. C. (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
  • 51
    • 15544364345 scopus 로고    scopus 로고
    • Analysis of ATP binding to CheA containing tryptophan substitutions near the active site
    • Stewart, R. C. (2005) Analysis of ATP binding to CheA containing tryptophan substitutions near the active site. Biochemistry 44, 4375-4385.
    • (2005) Biochemistry , vol.44 , pp. 4375-4385
    • Stewart, R.C.1
  • 52
    • 0024228682 scopus 로고
    • N-Terminal half of CheB is involved in methylesterase response to negative chemotactic stimuli
    • Stewart, R. C., and Dahlquist, F. W. (1988) N-Terminal half of CheB is involved in methylesterase response to negative chemotactic stimuli. J. Bacteriol. 170, 5728-5738.
    • (1988) J. Bacteriol , vol.170 , pp. 5728-5738
    • Stewart, R.C.1    Dahlquist, F.W.2
  • 53
    • 0033792542 scopus 로고    scopus 로고
    • Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain
    • Stewart, R. C., Jahreis, K., and Parkinson, J. S. (2000) Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain. Biochemistry 39, 13157-13165.
    • (2000) Biochemistry , vol.39 , pp. 13157-13165
    • Stewart, R.C.1    Jahreis, K.2    Parkinson, J.S.3
  • 54
    • 0032168668 scopus 로고    scopus 로고
    • TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli
    • Stewart, R. C., VanBruggen, R., Ellefson, D. D., and Wolfe, A. J. (1998) TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli. Biochemistry 37, 12269-12279.
    • (1998) Biochemistry , vol.37 , pp. 12269-12279
    • Stewart, R.C.1    VanBruggen, R.2    Ellefson, D.D.3    Wolfe, A.J.4
  • 55
    • 0000621729 scopus 로고    scopus 로고
    • in Escherichia coli and Salmonella
    • Neidhardt, F. C, Ed, pp, ASM Press, Washington, DC
    • Stock, J., and Surette, M. G. (1996) in Escherichia coli and Salmonella. Cellular and Molecular Biology (Neidhardt, F. C., Ed.) pp 1103-1129, ASM Press, Washington, DC.
    • (1996) Cellular and Molecular Biology , pp. 1103-1129
    • Stock, J.1    Surette, M.G.2
  • 56
    • 0027156598 scopus 로고
    • Intermolecular complementation of the kinase activity of CheA
    • Swanson, R. V., Bourret, R. B., and Simon, M. I. (1993) Intermolecular complementation of the kinase activity of CheA. Mol. Microbiol. 8, 435-441.
    • (1993) Mol. Microbiol , vol.8 , pp. 435-441
    • Swanson, R.V.1    Bourret, R.B.2    Simon, M.I.3
  • 57
    • 0027237735 scopus 로고
    • Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities
    • Swanson, R. V., Schuster, S. C., and Simon, M. I. (1993) Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities. Biochemistry 32, 7623-7629.
    • (1993) Biochemistry , vol.32 , pp. 7623-7629
    • Swanson, R.V.1    Schuster, S.C.2    Simon, M.I.3
  • 58
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among Bacteria and Archaea
    • Szurmant, H., and Ordal, G. W. (2004) Diversity in chemotaxis mechanisms among Bacteria and Archaea. Microbiol. Mol. Biol. Rev. 68, 301-319.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 59
    • 0028275837 scopus 로고
    • Kinetics of CheA autophosphorylation and dephosphorylation reactions
    • Tawa, P., and Stewart, R. C. (1994) Kinetics of CheA autophosphorylation and dephosphorylation reactions. Biochemistry 33, 7917-7924.
    • (1994) Biochemistry , vol.33 , pp. 7917-7924
    • Tawa, P.1    Stewart, R.C.2
  • 60
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: Bacterial chemotaxis
    • Wadhams, G. H., and Armitage, J. P. (2004) Making sense of it all: Bacterial chemotaxis. Nat. Rev. Mol. Cell Biol. 5, 1924-1937.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 1924-1937
    • Wadhams, G.H.1    Armitage, J.P.2
  • 61
    • 0023835316 scopus 로고
    • Asymmetry of tyrosyl-tRNA synthetase in solution
    • Ward, W. H. J., and Fersht, A. R. (1988) Asymmetry of tyrosyl-tRNA synthetase in solution. Biochemistry 27, 1041-1049.
    • (1988) Biochemistry , vol.27 , pp. 1041-1049
    • Ward, W.H.J.1    Fersht, A.R.2
  • 62
    • 0023677817 scopus 로고
    • Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-sites activity
    • Ward, W. H. J., and Fersht, A. R. (1988) Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-sites activity. Biochemistry 27, 5525-5530.
    • (1988) Biochemistry , vol.27 , pp. 5525-5530
    • Ward, W.H.J.1    Fersht, A.R.2
  • 63
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch, M. C. N., Mourey, L., Birck, C., and Samama, J.-P. (1997) Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat. Struct. Biol. 5, 25-29.
    • (1997) Nat. Struct. Biol , vol.5 , pp. 25-29
    • Welch, M.C.N.1    Mourey, L.2    Birck, C.3    Samama, J.-P.4
  • 64
    • 0027467850 scopus 로고
    • The short form of the CheA protein restores kinase activity an chemotactic ability to kinase-deficient mutants
    • Wolfe, A. J., and Stewart, R. C. (1993) The short form of the CheA protein restores kinase activity an chemotactic ability to kinase-deficient mutants. Proc. Natl. Acad. Sci. U.S.A. 90, 1518-1522.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 1518-1522
    • Wolfe, A.J.1    Stewart, R.C.2
  • 65
    • 0026322995 scopus 로고
    • Intermolecular complementation between two defective mutant signal-transducing receptors of Escherichia coli
    • Yang, Y., and Inouye, M. (1991) Intermolecular complementation between two defective mutant signal-transducing receptors of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88, 11057-11061.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 11057-11061
    • Yang, Y.1    Inouye, M.2
  • 66
    • 0030043573 scopus 로고    scopus 로고
    • Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
    • Zhou, H. J., McEvoy, M. M., Lowry, D. F., Swanson, R. V., Simon, M. I., and Dahlquist, F. W. (1996) Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry 35, 433-443.
    • (1996) Biochemistry , vol.35 , pp. 433-443
    • Zhou, H.J.1    McEvoy, M.M.2    Lowry, D.F.3    Swanson, R.V.4    Simon, M.I.5    Dahlquist, F.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.