PMID:14749334

Citation	Szurmant, H, Muff, TJ and Ordal, GW (2004) Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade. J. Biol. Chem. 279:21787-92
Abstract	Rapid restoration of prestimulus levels of the chemotactic response regulator, CheY-P, is important for preparing bacteria and archaea to respond sensitively to new stimuli. In an extension of previous work (Szurmant, H., Bunn, M. W., Cannistraro, V. J., and Ordal, G. W. (2003) J. Biol. Chem. 278, 48611-48616), we describe a new family of CheY-P phosphatases, the CYX family, that is widespread among the bacteria and archaea. These proteins provide another pathway, in addition to the ones involving CheZ of the gamma- and beta-proteobacteria (e.g. Escherichia coli) or the alternative CheY that serves as a "phosphate sink" among the alpha-proteobacteria (e.g. Sinorhizobium meliloti), for dephosphorylating CheY-P. In particular, we identify CheC, known previously to be involved in adaptation to stimuli in Bacillus subtilis, as a CheY-P phosphatase. Using an in vitro assay used previously to demonstrate that the switch protein FliY is a CheY-P phosphatase, we have shown that increasing amounts of CheC accelerate the hydrolysis of CheY-P. In vivo, a double mutant lacking cheC and the region of fliY that encodes the CheY-P binding domain is almost completely smooth swimming, implying that these cells contain very high levels of CheY-P. CheC appears to be primarily involved in restoring normal CheY-P levels following the addition of attractant, whereas FliY seems to act on CheY-P constitutively. The activity of CheC is relatively low compared to that of FliY, but we have shown that the chemotaxis protein CheD enhances the activity of CheC 5-fold. We suggest a model for how FliY, CheC, and CheD work together to regulate CheY-P levels in the bacterium.
Links	PubMed Online version:10.1074/jbc.M311497200
Keywords	Amino Acid Sequence; Asparagine/pharmacology; Bacillus subtilis/metabolism; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Chemotaxis; Dose-Response Relationship, Drug; Escherichia coli/metabolism; Gene Expression Regulation, Bacterial; Hydrolysis; Membrane Proteins/metabolism; Membrane Proteins/physiology; Models, Biological; Molecular Sequence Data; Mutation; Phenotype; Phosphorylation; Phylogeny; Plasmids/metabolism; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Signal Transduction; Time Factors
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:CHED		GO:0006935: chemotaxis	ECO:0000314:		P		in Bacillus subtilis CheC chemotaxis can be activated by CheD. CheD has no effect on CheY-P stability alone, but Fig 4 shows it enhances CheY-P hydrolysis in the presence of CheC. It was calculated that CheC is 5.3-fold more active in the presence than in the absence of CheD.	complete
BACSU:CHEC		GO:0051345: positive regulation of hydrolase activity	ECO:0000314:		P		See Results: CheC increases the Rate of CheY-P hydrolysis	complete CACAO 10403
BACSU:CHEC		GO:0050918: positive chemotaxis	ECO:0000315:		P		See Figure 5. Null mutant did not demonstrate swarming ability. Also see Figure 6 null mutant capillary assays.	complete CACAO 10404
BACSU:CHEC		GO:0004721: phosphoprotein phosphatase activity	ECO:0000314:		F		Dephosphorylation of CheY-P occurs through a hydrolysis reaction regulated by CheC. See Figure 3.	complete CACAO 10405
BACSU:CHEC	involved_in	GO:0050918: positive chemotaxis	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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