Myristoylation is an irreversible, post-translational protein modification found in animals, plants, fungi and viruses. In this protein modification a myristoyl group (derived from myristic acid) is covalently attached via an amide bond to the alpha-amino group of an N-terminal glycine residue of a nascent polypeptide. The modification is catalyzed by the enzyme N-myristoyltransferase, and occurs most commonly on glycine residues exposed during co-translational N-terminal methionine removal. Myristoylation also occurs post-translationally, for example when previously internal glycine residues become exposed by caspase cleavage during apoptosis. Myristoylation plays a vital role in membrane targeting and signal transduction in plant responses to environmental stress.

References

Podell S and Gribskovi M. Predicting N-terminal myristoylation sites in plant proteins. BMC Genomics 2004, 5:37.

Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ: Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000, 290:1761-1765.

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