Key result
RNAi silencing reveals unique spliceosomal Sm proteins bind U2 and U4 snRNAs in Trypanosoma brucei.
Identifies specific core Sm proteins (SSm) that bind only to a subset of spliceosomal snRNAs (U2 and U4) in Trypanosoma brucei.
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May guide antiparasitic drug design; leaves open whether SSm proteins are viable selective targets.
In eukaryotes the seven Sm core proteins bind to U1, U2, U4, and U5 snRNAs. In Trypanosoma brucei, Sm proteins have been implicated in binding both spliced leader (SL) and U snRNAs. In this study, we examined the function of these Sm proteins using RNAi silencing and protein purification. RNAi silencing of each of the seven Sm genes resulted in accumulation of SL RNA as well as reduction of several U snRNAs. Interestingly, U2 was unaffected by the loss of SmB, and both U2 and U4 snRNAs were unaffected by the loss of SmD3, suggesting that these snRNAs are not bound by the heptameric Sm complex that binds to U1, U5, and SL RNA. RNAi silencing and protein purification showed that U2 and U4 snRNAs were bound by a unique set of Sm proteins that we termed SSm (specific spliceosomal Sm proteins). This is the first study that identifies specific core Sm proteins that bind only to a subset of spliceosomal snRNAs.
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Tkacz et al. (2006) studied Trypanosoma brucei. RNAi silencing of Sm genes was evaluated on Accumulation of SL RNA and reduction of U snRNAs. RNAi silencing and protein purification revealed that U2 and U4 snRNAs in Trypanosoma brucei are bound by a unique set of specific spliceosomal Sm proteins (SSm).
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