Myristoylation
Myristoylation (also called N -myristylation or myristylation ) is the process by which myristic acid (myristate) is attached to the N -terminal glycine residue of proteins . The attachment of this fatty acid is very specific and is an important mostly cotranslational but also post-translational modification of proteins.
Myristic acid is irreversibly coupled to an N -terminal glycine by the so-called N-myristoyltransferase . This process usually takes place immediately after a specific proteolysis, i. H. Enzymes split the protein so that a peptide with N -terminal glycine is formed (often only the initial methionine is split off).
N -myristoylation mediates weak, reversible interactions with the cell membrane and other proteins. The transport and localization of proteins can also be controlled via myristoylation. An example of myristoylated proteins are the Src kinase family, several G proteins, and others. In plants , myristoylation also plays an important role in signal transduction in responding to stress.
literature
- TA Farazi, G. Waksman, JI Gordon : The biology and enzymology of protein N-myristoylation. In: J Biol Chem . 276 (43), Oct 26, 2001, pp. 39501-39504. PMID 11527981 .
- S. Podell, M. Gribskovi: Predicting N-terminal myristoylation sites in plant proteins. In: BMC Genomics. 5, 2004, p. 37.
- J. Zha, S. Weiler, KJ Oh, MC Wei, SJ Korsmeyer : Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. In: Science . 290, 2000, pp. 1761-1765.