PMID:20398208

Citation	Liarzi, O, Barak, R, Bronner, V, Dines, M, Sagi, Y, Shainskaya, A and Eisenbach, M (2010) Acetylation represses the binding of CheY to its target proteins. Mol. Microbiol. 76:932-43
Abstract	The ability of CheY, the response regulator of bacterial chemotaxis, to generate clockwise rotation is regulated by two covalent modifications - phosphorylation and acetylation. While the function and signal propagation of the former are widely understood, the mechanism and role of the latter are still obscure. To obtain information on the function of this acetylation, we non-enzymatically acetylated CheY to a level similar to that found in vivo, and examined its binding to its kinase CheA, its phosphatase CheZ and the switch protein FliM - its target at the flagellar switch complex. Acetylation repressed the binding to all three proteins. These results suggest that both phosphorylation and acetylation determine CheY's ability to bind to its target proteins, thus providing two levels of regulation, fast and slow respectively. The fast level is modulated by environmental signals (e.g. chemotactic and thermotactic stimuli). The slow one is regulated by the metabolic state of the cell and it determines, at each metabolic state, the fraction of CheY molecules that can participate in signalling.
Links	PubMed Online version:10.1111/j.1365-2958.2010.07148.x
Keywords	Acetylation; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Chemotaxis; Escherichia coli/metabolism; Escherichia coli/physiology; Lysine/genetics; Lysine/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:CHEY		GO:0018393: internal peptidyl-lysine acetylation	ECO:0000315:		P		Figure 3 shows that the double-mutant with mutations in lysine residues 92 and 122 exhibits significantly less acetylation than WT. This shows that lysine 92 and 122 residues are acetylated.	complete CACAO 5100
ECOLI:CHEY	involved_in	GO:0018393: internal peptidyl-lysine acetylation	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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