Structural Biochemistry/Proteins/Myristoylation

Myristoylation is an irreversible, co-translational (during translation) 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 amino acid of a nascent polypeptide. It is more common on glycine residues but also occurs on other amino acids. The modification is catalyzed by the enzyme N-myristoyltransferase (NMT), 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 also plays a vital role in membrane targeting and signal transduction in plant responses to environmental stress.


Podell S and Gribskov M. (2004) "Predicting N-terminal myristoylation sites in plant proteins", BMC Genomics, 5.

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