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Gene Review

ECs2592  -  chemotaxis regulatory protein CheY

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs2592


High impact information on ECs2592

  • We showed previously that phosphorylation of CheY is activated in reactions containing receptor, CheW, CheA, and CheY [6].
  • We have also found that CheZ, a protein that appears to antagonize CheY function in vivo, accelerates the hydrolysis of the phosphate on CheY [7].
  • A quaternary complex formed which consisted of the response regulator CheY, the histidine protein kinase CheA, a coupling protein CheW and a membrane-bound chemoreceptor Tar. Using various experimental conditions and mutant proteins, we have shown that the complex dissociates under conditions that favour phosphorylation of CheY [8].
  • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis [1].
  • The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site [1].

Chemical compound and disease context of ECs2592


Biological context of ECs2592


Anatomical context of ECs2592

  • In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior [2].
  • Helicobacter pylori possesses two CheY response regulators and a histidine kinase sensor, CheA, which are essential for chemotaxis and colonization of the gastric mucosa [17].
  • However, cells containing transducers and CheY failed to respond to attractants or repellents normally detected in the periplasm [18].
  • A plot of the fraction of the population that are tumbling versus the CheY concentration was hyperbolic, with half of the population tumbling at 30 microM (25,000 copies per cell) CheY monomers in the cytosol [19].

Associations of ECs2592 with chemical compounds

  • The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet [1].
  • Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD [2].
  • Here we report the co-crystal structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-) [20].
  • CheY can also use intermediary metabolites such as acetyl phosphate and carbamoyl phosphate as phospho-donors [21].
  • Both CheY and CheB use the N-phosphoryl group in phosphoramidate (NH2PO3(2-)) as a phospho-donor [21].

Analytical, diagnostic and therapeutic context of ECs2592


  1. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Stock, A.M., Mottonen, J.M., Stock, J.B., Schutt, C.E. Nature (1989) [Pubmed]
  2. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX. Park, S.Y., Chao, X., Gonzalez-Bonet, G., Beel, B.D., Bilwes, A.M., Crane, B.R. Mol. Cell (2004) [Pubmed]
  3. Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Stock, A., Koshland, D.E., Stock, J. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  4. 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., Crane, B.R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. FrzE of Myxococcus xanthus is homologous to both CheA and CheY of Salmonella typhimurium. McCleary, W.R., Zusman, D.R. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  6. The dynamics of protein phosphorylation in bacterial chemotaxis. Borkovich, K.A., Simon, M.I. Cell (1990) [Pubmed]
  7. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Hess, J.F., Oosawa, K., Kaplan, N., Simon, M.I. Cell (1988) [Pubmed]
  8. 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. Nature (1993) [Pubmed]
  9. Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. Sanders, D.A., Gillece-Castro, B.L., Stock, A.M., Burlingame, A.L., Koshland, D.E. J. Biol. Chem. (1989) [Pubmed]
  10. Elucidation of a PTS-carbohydrate chemotactic signal pathway in Escherichia coli using a time-resolved behavioral assay. Lux, R., Munasinghe, V.R., Castellano, F., Lengeler, J.W., Corrie, J.E., Khan, S. Mol. Biol. Cell (1999) [Pubmed]
  11. Atomic resolution structure of a succinimide intermediate in E.coli CheY. Simonovic, M., Volz, K. J. Mol. Biol. (2002) [Pubmed]
  12. High mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate. Silversmith, R.E. Biochemistry (2005) [Pubmed]
  13. Only one of the five CheY homologs in Vibrio cholerae directly switches flagellar rotation. Hyakutake, A., Homma, M., Austin, M.J., Boin, M.A., Häse, C.C., Kawagishi, I. J. Bacteriol. (2005) [Pubmed]
  14. Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY. Ramakrishnan, R., Schuster, M., Bourret, R.B. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  15. Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Swanson, R.V., Lowry, D.F., Matsumura, P., McEvoy, M.M., Simon, M.I., Dahlquist, F.W. Nat. Struct. Biol. (1995) [Pubmed]
  16. Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer. Sourjik, V., Berg, H.C. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  17. Helicobacter pylori possesses two CheY response regulators and a histidine kinase sensor, CheA, which are essential for chemotaxis and colonization of the gastric mucosa. Foynes, S., Dorrell, N., Ward, S.J., Stabler, R.A., McColm, A.A., Rycroft, A.N., Wren, B.W. Infect. Immun. (2000) [Pubmed]
  18. Reconstitution of signaling in bacterial chemotaxis. Wolfe, A.J., Conley, M.P., Kramer, T.J., Berg, H.C. J. Bacteriol. (1987) [Pubmed]
  19. Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli. Kuo, S.C., Koshland, D.E. J. Bacteriol. (1987) [Pubmed]
  20. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Zhao, R., Collins, E.J., Bourret, R.B., Silversmith, R.E. Nat. Struct. Biol. (2002) [Pubmed]
  21. Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Lukat, G.S., McCleary, W.R., Stock, A.M., Stock, J.B. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  22. Acetyladenylate plays a role in controlling the direction of flagellar rotation. Wolfe, A.J., Conley, M.P., Berg, H.C. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  23. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Bourret, R.B., Hess, J.F., Simon, M.I. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  24. Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering. Bourret, R.B., Drake, S.K., Chervitz, S.A., Simon, M.I., Falke, J.J. J. Biol. Chem. (1993) [Pubmed]
  25. Crystallization and preliminary characterization of CheY, a chemotaxis control protein from Escherichia coli. Volz, K., Beman, J., Matsumura, P. J. Biol. Chem. (1986) [Pubmed]
  26. Binding of the chemotaxis response regulator CheY to the isolated, intact switch complex of the bacterial flagellar motor: lack of cooperativity. Sagi, Y., Khan, S., Eisenbach, M. J. Biol. Chem. (2003) [Pubmed]
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