A rapid posttranslational myristylation of a 68-kD protein in D. discoideum.
Cells incubated with [3H]myristate were shown to rapidly and specifically acylate a 68-kD protein, p68, in a developmentally-regulated manner. The fatty acid incorporated into p68 was identified as myristate, and is linked to the protein via an amide bond, apparently to an NH2-terminal glycine. The acylation of p68 in D. discoideum displays some unusual properties. Unexpectedly, myristylation of p68 is a posttranslational event and occurs in the presence of inhibitors of protein synthesis. Another unusual finding was that although p68 is a stable protein, the acyl moiety is removed with a half time of approximately 15 min.
E. A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104.
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da Silva
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Klein
D000215:Acylation; D003513:Cycloheximide / Q000494:pharmacology; D004023:Dictyostelium / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D008970:Molecular Weight; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000494:pharmacology; D011499:Protein Processing, Post-Translational
D005656:Fungal Proteins; D006898:Hydroxylamines; D009227:Myristic Acids; D019814:Myristic Acid; D019811:Hydroxylamine; D003513:Cycloheximide; D010447:Peptide Hydrolases