Abstract
Small ubiquitin like modifier (SUMO) proteins are involved in many processes in eukaryotes. We here show that Trypanosoma brucei SUMO (Tb927.5.3210) modifies many proteins. The levels of SUMOylation were unaffected by temperature changes but were increased by severe oxidative stress. We obtained evidence that trypanosome homologues of the SUMO conjugating enzyme Ubc9 (Tb927.2.2460) and the SUMO-specific protease SENP (Tb927.9.2220) are involved in SUMOylation and SUMO removal, respectively.
Highlights
Small ubiquitin like modifier (SUMO) proteins have been found in almost all eukaryotes
Conjugation of SUMO to target proteins alters their functions in multiple ways, and it is central to a multitude of different cellular processes
Many proteins are SUMOylated in T. brucei To detect SUMOylated proteins, an antibody was raised to His-tagged TbSUMO produced in E. coli. (For details of all plasmid constructs see Table 1.) The anti-T. brucei SUMO antibody was insufficiently specific
Summary
Small ubiquitin like modifier (SUMO) proteins have been found in almost all eukaryotes. From the E2 conjugation enzyme, SUMO binds to a target lysine residue (Geiss-Friedlander & Melchior, 2007; Ulrich, 2009). This process is assisted by an E3 ligase. The paraflagellar rod protein PFR1 ( called PAR3) was suggested as a SUMO target by Western blot analysis and in vitro SUMOylation (Annoura et al, 2012) but again no SUMOylated peptide was found (Xu et al, 2013). In this paper we describe preliminary functional characterisation of further components of the SUMOylation system in T. brucei and investigate the effects of various stresses on protein SUMOylation
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