Functional homology of Bacillus subtilis methyltransferase II and Escherichia coli cheR protein.
A chemotaxis-related methyltransferase enzyme from Bacillus subtilis has been shown to methylate membrane-bound proteins in Escherichia coli in vitro. The methylated proteins are in the same molecular weight range as authentic E. coli methyl-accepting chemotaxis proteins. It was also shown that wild type E. coli cytoplasmic extract could methylate membrane proteins from B. subtilis in its methyl-accepting chemotaxis protein region. Cytoplasmic extracts from methyltransferase mutants of either species could methylate neither set of methyl-accepting proteins in vitro. The B. subtilis enzyme was incapable of methylating any of a group of soluble eucaryotic proteins. These data suggest functional homology between B subtilis methyltransferase II and E. coli cheR protein (chemotaxis methyltransferase) despite the evolutionary divergence between these two species.
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins; D002462:Cell Membrane / Q000201:enzymology; D002633:Chemotaxis; D004926:Escherichia coli / Q000378:metabolism*; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D008780:Methyltransferases / Q000378:metabolism*; D013045:Species Specificity; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D008780:Methyltransferases