Abstract:
:The location of the sites of methylation of the methyl-accepting chemotaxis proteins (MCP) of Escherichia coli has been investigated by trypsin digestion and mapping of the peptides. The two principal MCPs, MCP I and MCP II, were found to have very similar methyl-labeled peptide patterns. Each produced three major species of methylated peptide. Both MCPs migrate on high-resolution sodium dodecyl sulfate--polyacrylamide slab gels a a cluster of discrete protein bands. Each band produced one of the three major methylated peptides as the unique or dominant species. Progressive demethylation of the least acidic peptide produced, sequentially, the intermediate and most acidic peptides before complete loss of the methyl label. This is consistent with a single peptide backbone carrying from one to three methyl groups. The possible significance of three methyl-accepting sites in a single tryptic peptide is discussed.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chelsky D,Dahlquist FWdoi
10.1021/bi00507a051subject
Has Abstractpub_date
1981-02-17 00:00:00pages
977-82issue
4eissn
0006-2960issn
1520-4995journal_volume
20pub_type
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