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Identification of novel snRNA-specific Sm proteins that bind selectively to U2 and U4 snRNAs in Trypanosoma brucei

机译:鉴定选择性结合布鲁氏锥虫U2和U4 snRNA的新型snRNA特异性Sm蛋白

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摘要

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.
机译:在真核生物中,七个Sm核心蛋白与U1,U2,U4和U5 snRNA结合。在布鲁氏锥虫中,Sm蛋白已牵涉结合剪接的前导序列(SL)和U snRNA。在这项研究中,我们使用RNAi沉默和蛋白质纯化技术检查了这些Sm蛋白质的功能。七个Sm基因的每一个的RNAi沉默导致SL RNA的积累以及几个U snRNA的减少。有趣的是,U2不受SmB丢失的影响,U2和U4 snRNA均不受SmD3丢失的影响,这表明这些snRNA不受与U1,U5和SL RNA结合的七聚Sm复合物的束缚。 RNAi沉默和蛋白质纯化显示,U2和U4 snRNA被一组独特的Sm蛋白(我们称为SSm(特异性剪接Sm蛋白))结合。这是第一项鉴定仅结合一部分剪接snRNA的特定核心Sm蛋白的研究。

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