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The multisubunit eukaryotic initiation factor 3 (eIF3) plays multiple roles in translation but is poorly understood in trypanosomes. The putative subunits eIF3a and eIF3f of  Trypanosoma brucei  ( Tb IF3a and  Tb IF3f) were overexpressed and purified, and 11 subunits were identified,  Tb IF3a through l minus j, which form a tight complex. Both  Tb IF3a and  Tb IF3f are essential for the viability of  T. brucei . RNAi knockdown of either of them severely reduced total translation and the ratio of the polysome/80S peak area.  Tb IF3f and  Tb IF3a RNAi cell lines were modified to express tagged- Tb IF3a and - Tb IF3f, respectively. RNAi in combination with affinity purification assays indicated that both subunits are variably required for  Tb IF3 stability and integrity. The relative abundance of other subunits in the  Tb IF3f-tag complex changed little upon  Tb IF3a depletion; while only subunits  Tb IF3b, i, and e copurified comparably with  Tb IF3a-tag upon  Tb IF3f depletion. A genome-wide UV-crosslinking assay showed that several  Tb IF3 subunits have direct RNA-binding activity, with  Tb IF3c showing the strongest signal. In addition, CrPV IRES, but neither EMCV IRES nor HCV IRES, was found to mediate translation in  T. brucei . These results together imply that the structure of  Tb IF3 and the subunits function have trypanosome-specific features, although the composition is evolutionarily conserved.

The eIF3 complex of Trypanosoma brucei: composition conservation does not imply the conservation of structural assembly and subunits function