Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteins.
Sensory transduction in E. coli consists of two phases, excitation and adaptation, both of which involve the methyl-accepting chemotaxis proteins (MCPs). These molecules relay transmembrane signals and are reversibly methylated during adaptation of E. coli to environmental stimuli. Each MCP contains multiple sites of methylation, and we identified six of these sites in MCPI. Recently, a second covalent modification of MCPs has been identified, which is not methylation. This modification, designated CheB-dependent modification, is stimulated by repellents and causes a net increase in the negative charge of MCPI and MCPII by one or two charges. We demonstrate that one CheB modification occurs on the methyl-accepting methionine-and lysine-containing tryptic peptide in MCPI and MCPII, and the second CheB modification is on an arginine-containing tryptic peptide. The CheB modification allows three additional methyl groups to be incorporated into the methyl-accepting methionine-lysine peptide, while not actually creating all of these methylation sites. The two CheB modifications occur sequentially. A possible mechanism by which CheB modification permits additional methylations and the role of CheB modification in bacterial chemotaxis are discussed.
D001426:Bacterial Proteins / Q000502:physiology*; D002633:Chemotaxis; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D005798:Genes, Bacterial; D008745:Methylation; D010446:Peptide Fragments / Q000032:analysis; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D010446:Peptide Fragments