Cloning, expression, and characterization of the acyl-CoA-binding protein in African trypanosomes

Kenneth G. Milne, Michael A. J. Ferguson

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    Abstract

    African trypanosomes are shielded from their hosts' defenses by a coat of variant surface glycoprotein molecules, each of which is attached to the plasma membrane by a glycosylphosphatidylinositol anchor. During the later stages of glycosylphosphatidylinositol biosynthesis, myristic acid is incorporated into the anchor from the donor myristoyl-CoA by a series of unique fatty acid remodeling and exchange reactions. We have cloned and expressed a recombinant trypanosome acyl-CoA-binding protein that has a preference for binding relatively short chain acyl-CoAs and that has a high affinity for binding myristoyl-CoA (K-d = 3.5 x 10(-10) M). This protein enhances fatty acid remodeling of glycosylphosphatidylinositol precursors in the trypanosome cell-free system. We speculate that the trypanosome acyl-CoA-binding protein plays an active role in supplying myristoyl-CoA to the fatty acid remodeling machinery in the parasite.

    Original languageEnglish
    Pages (from-to)12503-12508
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume275
    Issue number17
    DOIs
    Publication statusPublished - 28 Apr 2000

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