In vitro methylation and demethylation of methyl-accepting chemotaxis proteins in Bacillus subtilis.
Bacillus subtilis responds to attractants by demethylating a group of integral membrane proteins referred to as methyl-accepting chemotaxis proteins (MCPs). We have studied the methylation and demethylation of these proteins in an in vitro system, consisting of membrane vesicles, and purified methyltransferase and methylesterase. The chemoattractant aspartate was found to inhibit methylation and stimulate demethylation of MCPs. Escherichia coli radiolabeled membranes in the presence of B. subtilis enzyme do not respond to aspartate by an increase demethylation rate. We also report that B. subtilis MCPs are multiply methylated, demethylation resulting in slower migrating proteins on sodium dodecyl sulfate-polyacrylamide gels.
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins; D002462:Cell Membrane / Q000201:enzymology; D002630:Chemotactic Factors / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D008970:Molecular Weight; D012436:S-Adenosylmethionine / Q000378:metabolism
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D012436:S-Adenosylmethionine