CHARACTERIZATION OF A BI-LOBE ASSOCIATED RANGAP TRYPANOSOMA BRUCEI

Abstract

Trypanosoma brucei is the causative agent of African trypanosomaisis. This single-cell parasite contains a single flagellum important for cell movement, division and morphogenesis. A bi-lobed structure locates at the proximal base of the single flagellum and is tightly linked to the flagellum. A leucine-rich repeats (LRR) containing protein TbLRRP1 present on the bilobe is essential for bilobe duplication, flagellar attachment and cell motility. To understand the molecular mechanism of TbLRRP1 and to further investigate the function of the bilobe, I used a yeast-two-hybrid screening to search for proteins interacting with TbLRRP1. Yeast-two-hybrid screening resulted in a number of potential binding candidates. A previously uncharacterized, putative Ran-binding domain containing protein was of particular interest. TbLRRP1 formed a functional complex with small GTPase Ran and a Ran-binding domain containing protein in T. brucei and was required for Ran activation. These findings provide new insight to the mechanistic of the bi-lobed structure.