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J Biol Chem, Vol. 273, Issue 12, 6595-6598, March 20, 1998
From the Skaggs Institute for Chemical Biology and Department of
Cell Biology, The Scripps Research Institute, La
Jolla, California 92037
N-terminal myristoylation is a
cotranslational lipid modification common to many signaling proteins
that often serves an integral role in the targeting and/or function of
these proteins. Myristoylation is catalyzed by an enzyme activity,
N-myristoyltransferase (NMT), which transfers myristic acid from
myristoyl coenzyme A to the amino group of a protein's N-terminal
glycine residue. While a single human NMT cDNA has been isolated
and characterized (hNMT-1), biochemical evidence has indicated the
presence of several distinct NMTs in vivo, often varying in
either apparent molecular weight and/or subcellular distribution. We
now report the cloning and characterization of a second, genetically
distinct human NMT (hNMT-2), as well as the isolation of the respective
mouse NMT homologue for each human enzyme. The mouse and human versions
of each NMT are highly homologous, displaying greater than 95% amino
acid sequence identity. Comparisons between the NMT-1 and NMT-2
proteins revealed reduced levels of sequence identity (76-77%),
indicating that NMT-1 and NMT-2 comprise two distinct families of
N-myristoyltransferases. Transient transfection of either
the hNMT-1 or hNMT-2 cDNA into COS-7 cells resulted in the
expression of high levels of NMT enzyme activity. Both hNMT-1 and
hNMT-2 were found to myristoylate several commonly studied peptide
substrates with similar, but distinguishable, relative selectivities.
Western analysis revealed that while hNMT-2 appeared as a single 65-kDa
protein in transfected COS-7 cells, hNMT-1 was processed to provide
four distinct protein isoforms ranging from 49 to 68 kDa in size.
Collectively, these studies demonstrate a heretofore unappreciated
level of genetic complexity underlying the enzymology of N-terminal
myristoylation and suggest that the specific inhibition or regulation
of either NMT in vivo may in turn allow for the selective
control of particular myristoylation-dependent cellular functions.
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