Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.
Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.
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DOI：
10.1016/j.cell.2016.04.018
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发表时间：
2016-05-19
期刊：
影响因子：
64.5
通讯作者：
Wellinger RJ
中科院分区：
文献类型：
--
作者：
Lemieux B;Laterreur N;Perederina A;Noël JF;Dubois ML;Krasilnikov AS;Wellinger RJ
端粒酶是一种核糖核蛋白酶，能使端粒DNA重排，维持基因组的完整性。端粒酶活性最低限度需要一个模板RNA和一个催化蛋白。体内端粒活性需要额外的蛋白质。在这里，我们报告的Pop 1，Pop 6和Pop 7蛋白，已知的RNase P和RNase MRP的组成部分，结合到酵母端粒酶RNA和端粒酶全酶的基本组成部分。Pop 1/Pop 6/Pop 7结合是特异性的，并且涉及与RNase P/MRP的RNA中的蛋白质结合结构域高度相似的RNA结构域。结果还表明，Pop 1/Pop 6/Pop 7的功能是在体内维持RNA上的必需组分Est 1和Est 2。一致地，添加Popl允许在体外用野生型端粒酶RNA重建端粒酶活性。因此，相同的伴侣模块允许从不相关的祖RNA进化出功能上和结构上明显不同的RNP、端粒酶和RNase P/MRP。
Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo. Here we report that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme. Pop1/Pop6/Pop7 binding is specific and involves an RNA domain that is highly similar to a protein-binding domain in the RNAs of RNase P/MRP. The results also show that Pop1/Pop6/Pop7 function to maintain the essential components Est1 and Est2 on the RNA in vivo. Consistently, addition of Pop1 allows for telomerase activity reconstitution with wild type telomerase RNA in vitro. Thus, the same chaperoning module has allowed the evolution of functionally and, remarkably, structurally distinct RNPs, telomerase and RNases P/MRP, from unrelated progenitor RNAs.