Chemotaxis proteins

Xiong J, Kurtz DM Jr, Ai J, Sanders-Loehr J. 2000. A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39 5117-25. 

S ATP -I- chemotaxis protein CheA <3> (sensory transduction in chemotaxis) [11]... 

Swanson, R.V. Sanna, M.G. Simon, M.L Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol., 178, 484-489 (1996)... 

C. The Chemotaxis Protein CheY from Escherichia colt.242... 

PriiB, B.M., Campbell, J.W., Van Dyk, T.K., Zhu, C., Kogan, Y. and Matsumura, P. (2003). FUiD/FlhC is a regulator of anaerobic respiration and the Entner-Doudoroff pathway through induction of the methyl-accepting chemotaxis protein Aer. J. Bacterial. 185, 534- 43. 

Since the function of CheZ is to dephosphorylate CheY P, thereby terminating its interaction with the switeh, one could expect that CheZ will act primarily on switch-bound CheY P and will be randomly distributed in the cell or localized near the switeh. However, none of these expectations was found to be correct. First, Bren et al. found that CheZ cannot act on switch-bound CheY P it can only act on free CheY P [134], This is the consequence of the overlap, discussed in Section 7.5.2, between the interfaces of CheY that bind FliM and CheZ. Second, the distribution of CheZ in the cell is not random by analyzing cells expressing a functional, full-length CheZ fused with GFP or YFP, it was recently found that at least some of the CheZ molecules are localized in clusters at the cells poles [147, 677], CheZ being bound to CheAs [147]. This observation suggests that CheZ, like all the other cytoplasmic chemotaxis proteins, can be attached to the receptor supramolecular complex via CheA. This situation suggests that CheZ may have two different functions in chemotaxis one—still unknown—fullilled by CheZ localized at the receptor supramolecular complex, and one—fulfilled by non-localized CheZ— to terminate the interaction of CheY P with the switch. 

The chemotaxis protein CheY was subsequently identified by both the whole-cell and reductionist approaches as the clockwise signal, i.e., as the molecule that interacts with the switch, thereby promoting clockwise rotation. In the whole-cell approach, second-site suppression analysis implied that CheY interacts with the switch (for reviews, see [56, 459]), and overproduction of CheY in a gutted strain generated clockwise rotation ([168] for a review, see reference [212]). In the reductionist approach, purified CheY inserted into cytoplasm-free envelopes caused some of the envelopes to rotate clockwise [594]. The absence of cytoplasmic chemotaxis proteins in the intact cells and the absence of cytoplasm in the envelopes indicated that the interaction of CheY with the switch is direct. Later biochemical studies demonstrated... 

Barak, R. and Eisenbach, M. (1992). Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31, 1821-1826. 

Barak, R., Welch, M., Yanovsky, A., Oosawa, K. and Eisenbach, M. (1992). Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch. Biochemistry 31,10099-10107. Barak, R. and Eisenbach, M. (1996). Regulation of interaction between signaling protein CheY and flagellar motor during bacterial chemotaxis. Curr. Top. Cell. Reg. 34, 137-158. 

Bourret, R.B., Hess, J.F. and Simon, M.I. (1990). Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc. Natl. Acad. Sd. U.S.A. 87, 41-45. 

Bren, A. and Eisenbach, M. (2000). How signals are heard during bacterial chemotaxis Protein-protein interactions in sensory signal propagation./. Bacteriol. 182, 6865-6873. 

Brooun, A., Bell, J., Freitas, T., Larsen, R.W. and Alam, M. (1998). An archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins. J. Bacterial. 180, 1642-1646. 

Clarke, S., Sparrow, K., Ranasenko, S. and Koshland, D.E., Jr. (1980). In vitro methylation of bacterial chemotaxis proteins Characterization of protein methyl-transferase activity in crude extracts of Salmonella typhimurium. J. Supramol. Struct. 13, 315-328. 

Djordjevic, S. and Stock, A.M. (1998). Structural analysis of bacterial chemotaxis proteins Components of a dynamic signaling system./ Struct. Biol. 124,189-200. Doetsch, R.N. and Seymour, W.F. (1970). Negative chemotaxis in bacteria. Life Sci. 9,1029-1037. 

Engstrom, P. and Hazelbauer, G.L. (1982). Methyl-accepting chemotaxis proteins are distributed in the membrane independently from basal ends of bacterial flagella. Biochim. Biophys. Acta 686, 19-26. 

Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC. J. Bacterial. 180, 4475- 480. 

Gestwicki, J.E., Lamanna, A.C., Harshey, R.M., McCarter, L.L., Kiessling, L.L. and Adler, J. (2000). Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea. J. Bacterial. 182, 6499-6502. 

Hanlon, D.W and Ordal, G.W. (1994). Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis. J. Biol. Chem. 269, 14038-14046. 

Kehry, M.R., Bond, M.W., HunkapiUer, M.W. and Dahlquist, F.W. (1983). Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proc. Natl. Acad. Sci. U.S.A. 80,... 

Kleene, S.J., Hobson, A.C. and Adler, J. (1979). Attractants and repellents influence methylation and demethylation of methyl-accepting chemotaxis proteins in an extract of Escherichia coli. Proc. Nad. Acad. Sci. U.S.A. 76, 6309-6313. 

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. 

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