Protein fatty acid acylation: Enzymatic synthesis of an N-myristoylglycyl peptide

D. Towler, L. Glaser

Research output: Contribution to journalArticle

79 Scopus citations

Abstract

Incubation of Saccharomyces cerevisiae strain JR153 with either [3H]myristate or [3H]palmitate demonstrates the synthesis of proteins that contain covalently bound fatty acids. A unique set of proteins is labeled by each fatty acid. Detailed analysis of a 20-kDa protein labeled with myristic acid demonstrates that myristate is linked to the amino-terminal glycine. We describe an enzymatic activity in yeast that will transfer myristic acid to the amino terminus of the octapeptide Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg, whose sequence was derived from a known N-myristoylated acyl protein, the catalytic subunit of cAMP-dependent protein kinase of bovine cardiac muscle. The acylation reaction is dependent on ATP and CoA, is enriched in a crude membrane fraction, and will use myristate but not palmitate as the acyl donor. Specificity of the glycyl peptide substrate is demonstrated by the observation that other glycyl peptides do not competitively inhibit myristoylation of Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg.

Original languageEnglish (US)
Pages (from-to)2812-2816
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number9
DOIs
StatePublished - Jan 1 1986

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