Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma brucei.

ABSTRACT:

Background

Arginine 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.

Results

We identified a protein containing N-LIP an

SUBMITTER: Pelletier M 

PROVIDER: S-EPMC3654991 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature