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        Analysis of Myristoylated and Palmitoylated Src Family Proteins

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        Several hundred viral and cellular proteins have been shown to be covalently modified by fatty acids (1 3 ). The two most common modifications, myristoylatron and palmitoylatron, differ with respect to the type and chemical nature of fatty acid attachment to the polypeptide backbone. Most proteins destined to become N-myrrstoylated contain the sequence: Met-Gly-X-X-X-Ser/Thr at their N-terminn. After the initrating methionine is removed, the 14-carbon fatty acid myristate is attached via amide linkage to the N-terminal glycme residue. The reaction occurs cotranslationally and is catalyzed by the soluble enzyme N-myristoyl transferase (NMT). NMT exhibits strict specificity for an N-terminal glycine and mutation of this glycine to alanme abrogates myristoylation. In contrast, palmitoylated proteins contam the 16-carbon fatty acid palintiate attached via throester linkage to one or more cysteme residues. Palmitoylation is a posttranslational reactron that appears to be mediated by a membrane-bound palmitoyl acyl transferase. Unlike myristoylation, whrch is generally a relatively stable modification, palmitoylatron can be reversed by the action of thioesterases. Dynamic palmitoylation has recently been shown to play key roles in the regulation of protein localization and function.
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