PMID:11553614

Citation	Karatan, E, Saulmon, MM, Bunn, MW and Ordal, GW (2001) Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis. J. Biol. Chem. 276:43618-26
Abstract	In the Gram-positive soil bacterium Bacillus subtilis, the chemoreceptors are coupled to the central two-component kinase CheA via two proteins, CheW and CheV. CheV is a two-domain protein with an N-terminal CheW-like domain and a C-terminal two-component receiver domain. In this study, we show that CheV is phosphorylated in vitro on a conserved aspartate in the presence of phosphorylated CheA (CheA-P). This reaction is slower compared with the phospho-transfer reaction between CheA-P and one other response regulator of the system, CheB. CheV-P is also highly stable in comparison with CheB-P. Both of these properties are more pronounced in the full-length protein compared with a truncated form composed only of the receiver domain, that is, deletion of the CheW-like domain results in increase in the rate of the phospho-transfer reaction and decrease in stability of the phosphorylated protein. Phosphorylation of CheV is required for adaptation to the addition of the chemoattractant asparagine. In tethered-cell assays, strains expressing an unphosphorylatable point mutant of cheV or a truncated mutant lacking the entire receiver domain are severely impaired in adaptation to the addition of asparagine. Both of these strains, however, show near normal counterclockwise biases, suggesting that in the absence of the attractant the chemoreceptors are efficiently coupled to CheA kinase by the mutant CheV proteins. Inability of the CheW-like domain of CheV to support complete adaptation to the addition of asparagine also suggests that unlike CheW, this domain by itself may lead to the formation of signaling complexes that stay overactive in the presence of the attractant. A possible structural basis for this feature is discussed.
Links	PubMed Online version:10.1074/jbc.M104955200
Keywords	Adaptation, Physiological/physiology; Amino Acid Sequence; Bacillus subtilis/metabolism; Bacillus subtilis/physiology; Bacterial Proteins; Chemotactic Factors/chemistry; Chemotactic Factors/metabolism; Chemotaxis; Molecular Sequence Data; Phosphorylation; Sequence Homology, Amino Acid
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:CHEV		GO:0006935: chemotaxis	ECO:0000315:		P		Figure 5 shows the behavioral analysis of various strains in response to addition and removal of asparagine. Tethered-cell assays were performed and the arrows represent the addition and removal of asparagine.	complete
BACSU:CHEV		GO:0000160: phosphorelay signal transduction system	ECO:0000315:		P		See Figure 1: Phospho-transfer from CheA to wild-type and mutant CheV proteins.	complete
BACSU:CHEV		GO:0005622: intracellular	ECO:0000314:		C		Figure 3 shows that more CheA-P was transfered at both temperatures than CheB. This can be proven by the darkness of the band.	complete CACAO 5053
BACSU:CHEV		GO:0000160: two-component signal transduction system (phosphorelay)	ECO:0000314:		P		Figure 2 shows the rate of phoshotranser reactions between CheA-P and CheV.	complete
BACSU:CHEB		GO:0000155 phosphorelay sensor kinase activity: chemotaxis	ECO:0000315:		P		See Figure 3: Phospho-transfer between CheA-P and CheB.	complete
BACSU:CHEB		GO:0006935: chemotaxis	ECO:0000315:		P		Figure 3 shows the phospho-transfer between CheA-P and CheB. Reactions were separated by electrophoresis on a 10% SDS-polyacrylamide gel.	complete
BACSU:CHEA		GO:0000155: phosphorelay sensor kinase activity	ECO:0000315:		F		See Figure 1: Phospho-transfer from CheA to wild-type and mutant CheV proteins, and Figure 3: Phospho-transfer between CheA-P and CheB.	complete CACAO 10497

References

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