Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites.
Two-dimensional analysis of tryptic peptides from [35S]methionine-labeled methyl-accepting chemotaxis proteins, MCP I and MCP II, demonstrates a high degree of homology between the two proteins. After the methylation sites were labeled with S-adenosyl-L-methyl-3H]methionine, peptides of three distinct migrations in each protein were found to carry a methyl group. These multiple methylations appear to be responsible in part for the observed multiple banding patterns on sodium dodecyl sulfate/polyacrylamide slab gels.
D001426:Bacterial Proteins / Q000378:metabolism*; D002633:Chemotaxis; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000502:physiology*; D008745:Methylation; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis
D001426:Bacterial Proteins; D010446:Peptide Fragments