What question did this study set out to answer?

To explore the process of protein N-myristoylation, its mechanism, and biological significance in eukaryotic cells.

May 1, 1991Journal of Biological Chemistry293 citationsOpen Access

Protein N-myristoylation

JGJeffrey I. Gordon RDRobert J. Duronio DRDavid A. Rudnick

Key Points

To explore the process of protein N-myristoylation, its mechanism, and biological significance in eukaryotic cells.
Describes the covalent attachment mechanism of myristic acid to proteins.
Explains the role of N-myristoyltransferase in transferring myristate from myristoylCoA to proteins.
Examines the evolution and substrate specificity of N-myristoyltransferase among eukaryotes.
N-myristoylation occurs during protein synthesis through an amide bond formation.
N-myristoylproteins are involved in critical cellular functions including signal transduction and vesicular trafficking.
The substrate specificity of N-myristoyltransferase shows evolutionary conservation but divergence in peptide substrates across eukaryotic groups.

Abstract

Protein N-myristoylation refers to the covalent attachment of myristic acid, a 14-carbon saturated fatty acid (C14:0), to the N-terminal glycine of proteins. Linkage occurs via an amide bond and takes place as proteins are being synthesized. N-myristoylproteins have varied intracellular destinations, and are involved in myriad cellular functions ranging from signal transduction to protein and vesicular trafficking. N-myristoylproteins are encountered in members of all kingdoms of the eukaryotic domain (Protist, Fungi, Plant, and Animal), but are not produced by members of Bacteria or Archaea. MyristoylCoA: protein N-myristoyltransferase (Nmt), E.C. 2.3.1.97, a member of the GCN5 acetyltransferase (GNAT) superfamily, is responsible for catalyzing the transfer of myristate from myristoylCoA to proteins. While the acylCoA substrate specificity of Nmt has been highly conserved during evolution, its peptide substrate specificities have diverged among eukaryotes.

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