Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma bruceiReportar como inadecuado

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BMC Microbiology

, 13:101

Microbial biochemistry, physiology and metabolism


BackgroundArginine methylation is a post-translational modification that expands the functional diversity of proteins. Kinetoplastid parasites contain a relatively large group of protein arginine methyltransferases PRMTs compared to other single celled eukaryotes. Several T. brucei proteins have been shown to serve as TbPRMT substrates in vitro, and a great number of proteins likely to undergo methylation are predicted by the T. brucei genome. This indicates that a large number of proteins whose functions are modulated by arginine methylation await discovery in trypanosomes. Here, we employed a yeast two-hybrid screen using as bait the major T. brucei type I PRMT, TbPRMT1, to identify potential substrates of this enzyme.

ResultsWe identified a protein containing N-LIP and C-LIP domains that we term TbLpn. These domains are usually present in a family of proteins known as lipins, and involved in phospholipid biosynthesis and gene regulation. Far western and co-immunoprecipitation assays confirmed the TbPRMT1-TbLpn interaction. We also demonstrated that TbLpn is localized mainly to the cytosol, and is methylated in vivo. In addition, we showed that, similar to mammalian and yeast proteins with N-LIP and C-LIP domains, recombinant TbLpn exhibits phosphatidic acid phosphatase activity, and that two conserved aspartic acid residues present in the C-LIP domain are critical for its enzymatic activity.

ConclusionsThis study reports the characterization of a novel trypanosome protein and provides insight into its enzymatic activity and function in phospholipid biosynthesis. It also indicates that TbLpn functions may be modulated by arginine methylation.

KeywordsKinetoplastid Lipin Arginine methylation Phosphatidic acid phosphatase Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-13-101 contains supplementary material, which is available to authorized users.

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Autor: Michel Pelletier - Alyssa S Frainier - Dominic N Munini - Jenna M Wiemer - Amber R Karpie - Jeff J Sattora


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