S-myristoylation of a glycosylphosphatidylinositol-specific phospholipase C in Trypanosoma brucei

被引:29
|
作者
Armah, DA [1 ]
Mensa-Wilmot, K [1 ]
机构
[1] Univ Georgia, Dept Cellular Biol, Athens, GA 30602 USA
关键词
D O I
10.1074/jbc.274.9.5931
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Covalent modification with lipid can target cytosolic proteins to biological membranes. With intrinsic membrane proteins, the role of acylation can be elusive. Herein, we describe covalent lipid modification of an integral membrane glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) from the kinetoplastid Trypanosoma brucei. Myristic acid was detected on cysteine residue(s) (i.e. thiomyristoylation). Thiomyristoylation occurred both co- and post-translationally Acylated GPI-PLC was active against variant surface glycoprotein (VSG). The half-life of fatty acid on GPI-PLC was 45 min, signifying the dynamic nature of the modification. Deacylation in vitro decreased activity of GPI-PLC 18-30-fold. Thioacylation, from kinetic analysis, activated GPI-PLC by accelerating the conversion of a GPI-PLC VSG complex to product. Reversible thioacylation is a novel mechanism for regulating the activity of a phospholipase C.
引用
收藏
页码:5931 / 5938
页数:8
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