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In Trypanosoma brucei, the U2-specific U2B'' protein interacts with U2-40K and the Sm16.5K/15K subcomplex to form a high-affinity binding complex, differing from the mammalian system.
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Divergence from mammalian spliceosome assembly may enable selective antiparasitic strategies; leaves open validation and clinical translation.
The processing of polycistronic pre-mRNAs in trypanosomes requires the spliceosomal small ribonucleoprotein complexes (snRNPs) U1, U2, U4/U6, U5, and SL, each of which contains a core of seven Sm proteins. Recently we reported the first evidence for a core variation in spliceosomal snRNPs; specifically, in the trypanosome U2 snRNP, two of the canonical Sm proteins, SmB and SmD3, are replaced by two U2-specific Sm proteins, Sm15K and Sm16.5K. Here we identify the U2-specific, nuclear-localized U2B'' protein from Trypanosoma brucei. U2B'' interacts with a second U2 snRNP protein, U2-40K (U2A'), which in turn contacts the U2-specific Sm16.5K/15K subcomplex. Together they form a high-affinity, U2-specific binding complex. This trypanosome-specific assembly differs from the mammalian system and provides a functional role for the Sm core variation found in the trypanosomal U2 snRNP.
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Preußer et al. (2009) studied this question. In Trypanosoma brucei, the U2-specific U2B'' protein interacts with U2-40K and the Sm16.5K/15K subcomplex to form a high-affinity binding complex, differing from the mammalian system.
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