Key result
SF3a60 is essential for Trypanosoma brucei cell viability and interacts with SF3a120, SF3a66, and SAP130, although its depletion had no detectable effect on trans-splicing.
SF3a60 is an essential nuclear protein in T. brucei that interacts with other spliceosomal components, but its depletion does not detectably impair trans-splicing prior to cell death.
SF3a60 is essential for T. brucei viability independent of trans-splicing; leaves open its utility as a selective antiparasitic target.
Trypanosoma brucei relies on Spliced leader trans splicing to generate functional messenger RNAs. Trans splicing joins the specialized SL exon from the SL RNA to pre-mRNAs and is mediated by the trans-spliceosome, which is made up of small nuclear ribonucleoprotein particles and non-snRNP factors. Although the trans spliceosome is essential for trypanosomatid gene expression, not all spliceosomal protein factors are known and of these, only a few are completely characterized. In this study, we have characterized the trypanosome Splicing Factor, SF3a60, the only currently annotated SF3a component. As expected, epitope-tagged SF3a60 localizes in the trypanosome nucleus. SF3a60 is essential for cell viability but its depletion seem to have no detectable effect on trans-splicing. In addition, we used SF3a60 as bait in a Yeast-2-hybrid system screen and identified its interacting protein factors. The interactions with SF3a120, SF3a66 and SAP130 were confirmed by tandem affinity purification and mass spectrometry.
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Nyambega et al. (2014) studied Trypanosoma brucei (Basic Science). SF3a60 characterization and RNAi depletion vs. Uninduced cells was evaluated on Cell viability and trans-splicing activity. SF3a60 is essential for Trypanosoma brucei cell viability and interacts with SF3a120, SF3a66, and SAP130, although its depletion had no detectable effect on trans-splicing.
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