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. 1980 May;77(5):2434-8.
doi: 10.1073/pnas.77.5.2434.

Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites

D Chelsky, F W Dahlquist

Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites

D Chelsky et al. Proc Natl Acad Sci U S A. 1980 May.

Abstract

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.

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