Abstract:
:The peptide portion of the lipopeptide isolated from bovine myelin basic protein contained glycine, lysine, and serine in a 2:1:1 molar ratio as determined by amino acid analysis. The N-terminus of the peptide was determined to be glycine. The tetrapeptide Gly53-Ser-Gly-Lys56 was the only segment of myelin basic protein that matched the above two characteristics. This tetrapeptide is highly conserved among the myelin basic proteins sequenced so far. After the selective degradation of the lipopeptide, phosphoserine was identified in the acid hydrolysate, thus indicating that Ser-54 of myelin basic protein in bovine brain is the site of attachment of polyphosphoinositide. Interestingly, serine-54 of myelin basic protein can be phosphorylated by the endogenous protein kinase myelin. However, myelin basic protein phosphorylated by the catalytic subunit of an exogenous soluble protein kinase failed to produce radioactively labeled lipopeptide. Hence the endogenous enzymes of myelin are thought to be involved in the formation of the covalent linkage between polyphosphoinositide and myelin basic protein. The conservation in sequence suggests a possible important structural role for the "phospholipidation" of myelin basic protein.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chang PC,Yang JC,Fujitaki JM,Chiu KC,Smith RAdoi
10.1021/bi00357a059subject
Has Abstractpub_date
1986-05-06 00:00:00pages
2682-6issue
9eissn
0006-2960issn
1520-4995journal_volume
25pub_type
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