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Papers In Press, published online ahead of print December 17, 2002
Biological Sciences, Imperial College London, London SW7 2AZ
Corresponding Author: d.smith{at}ic.ac.uk
Co-translational modification of eukaryotic proteins by N-myristoylation aids subcellular targeting and protein-protein interactions. The enzyme that catalyses this process, N-myristoyl transferase, has been characterised in the kinetoplastid protozoan parasites, Leishmania and Trypanosoma brucei. In L. major, the single copy NMT gene is constitutively expressed in all parasite stages as a 48.5kDa protein that localizes to both membrane and cytoplasmic fractions. Leishmania NMT myristoylates the target acylated Leishmania protein, HASPA, when both are co-expressed in E. coli. Gene targeting experiments have shown that NMT activity is essential for viability in Leishmania. In addition, over-expression of NMT causes gross changes in parasite morphology, including the sub-cellular accumulation of lipids, leading to cell death. This phenotype is more extreme than that observed in Saccharomyces cerevisiae, in which over-expression of NMT activity has no obvious effects on growth kinetics or cell morphology. RNA interference assays in T. brucei have confirmed that NMT is also an essential protein in both life cycle stages of this second kinetoplastid species, suggesting that this enzyme may be an appropriate target for the development of anti-parasitic agents.
J. Biol. Chem, 10.1074/jbc.M211391200
Submitted on November 7, 2002
Revised on December 10, 2002
Accepted on December 17, 2002
Myristoyl CoA: protein N-myristoyltransferase: an essential enzyme and potential drug target in kinetoplastid parasites
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