Characterization of Sm-like proteins in yeast and their association with U6 snRNA
Characterization of Sm-like proteins in yeast and their association with U6 snRNA
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DOI：
10.1093/emboj/18.15.4321
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发表时间：
1999-08-02
期刊：
影响因子：
11.4
通讯作者：
Beggs, JD
中科院分区：
文献类型：
--
作者：
Mayes, AE;Verdone, L;Beggs, JD
7种Sm蛋白与U1、U2、U4和U5剪接体snRNAs结合，影响snRNP的生物发生。在这里，我们描述了一组新的sm样（Lsm）蛋白，它们彼此相互作用并与U6 snRNA相互作用，七个Lsm蛋白与先前表征的Lsm4p （Uss1p）共免疫沉淀，并在双杂交分析中相互作用。游离的U6和U4/U6双工rna与7种对U6 snRNA的稳定积累至关重要的Lsm蛋白共同免疫沉淀，对Lsm缺失菌株的U4/U6双工rna和U4/U6 U5三工snRNA的分析表明，Lsm蛋白可能在剪合体复合物的结合-解离循环中促进U6 snRNP的构象重排。因此，Lsm蛋白形成的复合物在其RNA结合和功能上不同于典型的Sm复合物。我们讨论了其他Lsm复合物的可能存在和功能，包括它们参与mrna前剪接以外的过程的可能性。
Seven Sm proteins associate with U1, U2, U4 and U5 spliceosomal snRNAs and influence snRNP biogenesis. Here we describe a novel set of Sm-like (Lsm) proteins in Saccharomyces cerevisiae that interact with each other and with U6 snRNA, Seven Lsm proteins coimmunoprecipitate with the previously characterized Lsm4p (Uss1p) and interact with each other in two-hybrid analyses. Free U6 and U4/U6 duplexed RNAs co-immunoprecipitate with seven of the Lsm proteins that are essential for the stable accumulation of U6 snRNA, Analyses of U4/U6 di-snRNPs and U4/U6 U5 tri-snRNPs in Lsm-depleted strains suggest that Lsm proteins may play a role in facilitating conformational rearrangements of the U6 snRNP in the association-dissociation cycle of spliceosome complexes. Thus, Lsm proteins form a complex that differs from the canonical Sm complex in its RNA association(s) and function. We discuss the possible existence and functions of alternative Lsm complexes, including the likelihood that they are involved in processes other than pre-mRNA splicing.