The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage
The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage
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DOI：
10.1038/nsmb936
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发表时间：
2005-06-01
影响因子：
16.8
通讯作者：
Scadden, ADJ
中科院分区：
文献类型：
--
作者：
Scadden, ADJ
长的完美双链RNA（dsRNA）分子在各种细胞途径中发挥作用。dsRNA可以通过作用于RNA的腺苷脱氨酶（ADAR）进行广泛的共价修饰（超编辑），导致高达50%的腺苷残基转化为肌苷（I）。或者，dsRNA可以触发RNA干扰（RNAi），导致同源mRNA的沉默。这两种途径以前被证明是拮抗的。我们发现了阿达尔和RNAi途径的组分之间的一种新的相互作用。Tudor葡萄球菌核酸酶（Tudor-SN）是RNA诱导沉默复合物的一个亚基，是RNAi机制的核心。在这里，我们表明Tudor-SN特异性地与含有多个I.U和U.I对的模型超编辑dsRNA底物相互作用并促进其切割。这种相互作用表明，这两种途径之间存在一种新的、出乎意料的相互作用，这种相互作用比相互拮抗更复杂。
Long perfect double-stranded RNA ( dsRNA) molecules play a role in various cellular pathways. dsRNA may undergo extensive covalent modification (hyper-editing) by adenosine deaminases that act on RNA (ADARs), resulting in conversion of up to 50% of adenosine residues to inosine ( I). Alternatively, dsRNA may trigger RNA interference (RNAi), resulting in silencing of the cognate mRNA. These two pathways have previously been shown to be antagonistic. We show a novel interaction between components of the ADAR and RNAi pathways. Tudor staphylococcal nuclease (Tudor-SN) is a subunit of the RNA-induced silencing complex, which is central to the mechanism of RNAi. Here we show that Tudor-SN specifically interacts with and promotes cleavage of model hyper-edited dsRNA substrates containing multiple I.U and U.I pairs. This interaction suggests a novel unsuspected interplay between the two pathways that is more complex than mutual antagonism.