Identification and characterization of recombinant and native rat myristoyl-CoA: protein N-myristoyltransferases

Molecular and Cellular Biochemistry
Vincent RiouxPhilippe Legrand

Abstract

Compared to other species that possess a single functional myristoyl-CoA: protein N-myristoyltransferase gene copy, human, mouse and cow possess 2 NMT genes, and more than 2 protein isoforms. In mammals, the contribution of each gene transcript to multiple protein isoform expression and enzyme activity remains unclear. In order to get new insight on their respective physiological role, we have cloned and characterized the two rat NMT cDNAs. Rat NMT1 and NMT2 cDNAs contain 1491 and 1590 nucleotides, respectively, with high identity with their mouse homologues. Polypeptide sequences exhibited 68.1% identity between NMT1 and 2. Recombinant rat NMT1 and 2 showed major immunoreactive forms at 66 and 50 kDa, although NMT2 is 33-amino acid longer than NMT1. Both proteins exhibited functional myristoyltransferase activity but NMT2 appeared to be 4-time less active than NMT1. Studies of native protein expression revealed that the level and sizes of NMT proteins greatly vary among rat tissues although NMT1 and 2 did not display tissue specific expression at the mRNA level. Altogether, these results suggest that NMT2 may contribute little to total NMT activity levels in vivo.

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Citations

Jun 15, 2007·American Journal of Medical Genetics. Part a·Fabiola Quintero-RiveraDavid J Harris
Mar 8, 2008·ChemMedChem·Paul W BowyerKatherine A Brown
Dec 20, 2007·Current Opinion in Clinical Nutrition and Metabolic Care·Vincent Rioux, Philippe Legrand
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