Arginine Methylation of TbLpn, a Trypanosome Lipin Homologue, by TbPRMT Enzymes

Abstract

Phospholipids biosynthesis, particularly phosphatidylcholine (PC) and phosphatidylethanolamine (PE) plays a major role in the survival of T.brucei. Of great importance is the fact that, as opposed to other parasitic organisms, trypanosomes synthesize phospholipids de novo. Although the pathways for phospholipids biosynthesis have not been very well characterized, recent data have helped to better understand how trypanosomes are able to assemble phospholipids. Previous work in our lab has shown that a protein, termed TbLpn, is a phosphatidic acid phosphatase potentially involved in phospholipid biosynthesis in T.brucei. In addition, TbLpn contains methylated arginine residues and interacts with T.brucei major Protein Arginine Methyltransferases, TbPRMT7. The major focus of my project is to identify the effect of TbLpn methylation by TbPRMT7 on its enzymatic activity and cellular localization.