Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs
Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs
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DOI：
10.1093/emboj/cdf585
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发表时间：
2002-11-01
期刊：
影响因子：
11.4
通讯作者：
Fischer, U
中科院分区：
文献类型：
--
作者：
Meister, G;Fischer, U
虽然剪接体Sm蛋白可以在体外自发地组装到UsnRNA上，但这一过程需要体内的辅助因素。SMN是参与脊髓性肌萎缩的蛋白质，是含有Sm蛋白的复合物的一部分，并作为该反应的关键因子。在这里，我们在体外重建了SMN依赖的UsnRNP组装。我们证明了SMN复合物是组装反应的必要和充分条件。PRMT 5复合物，以前涉及甲基化和存储的Sm蛋白，与SMN复合物相互作用，并增强其活性的ATP依赖性的方式。这些数据揭示了SMN-PRMT 5复合物作为一种功能实体，促进剪接体UsnRNP和潜在的其他RNA-蛋白质复合物的辅助组装。
Although spliceosomal Sm proteins can assemble spontaneously onto UsnRNA in vitro, this process requires assisting factors in vivo. SMN, the protein involved in spinal muscular atrophy, is part of a complex that contains the Sm proteins and serves as a critical factor for this reaction. Here, we have reconstituted the SMN-dependent assembly of UsnRNPs in vitro. We demonstrate that the SMN complex is necessary and sufficient for the assembly reaction. The PRMT5 complex, previously implicated in methylation and storage of Sm proteins, interacts with the SMN complex and enhances its activity in an ATP-dependent manner. These data uncover the SMN-PRMT5 complex as a functional entity that promotes the assisted assembly of spliceosomal UsnRNPs, and potentially other, RNA-protein complexes.