RNase II The finer details of the Modus operandi of a molecular killer
RNase II The finer details of the Modus operandi of a molecular killer
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DOI：
10.4161/rna.7.3.11490
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发表时间：
2010-05-01
期刊：
影响因子：
4.1
通讯作者：
Barbas, Ana
中科院分区：
文献类型：
--
作者：
Arraiano, Cecilia M.;Matos, Rute G.;Barbas, Ana
RNase II酶家族是普遍存在的，在所有类型的RNA的加工、降解和质量控制中起着至关重要的作用。这些核糖核酸外切酶从3 '端降解RNA，释放5'-核苷酸单磷酸。在原核生物中，RNase II和RNase R具有参与RNA结合的两个N-末端CSD和一个C-末端S1结构域，以及中央催化RNB结构域。在真核生物中，Rrp 44 p/Dis 3是具有类似模块组织的RNase II样蛋白，其是外泌体中唯一具有催化活性的核酸酶，外泌体是RNA代谢的关键复合物。本文综述了近年来在RNase II降解机制研究方面的进展，包括RNase II的突变分析及其催化和RNA亲和性的表征。我们特别强调了E。coli RNase II，但功能和结构研究之间的协同作用表明，我们的研究结果对理解其他RNase II家族成员的类似作用模式具有意义。
The RNase II family of enzymes is ubiquitous and has crucial roles in the processing, degradation and quality control of all types of RNA. These exoribonucleases processively degrade RNA from the 3'-end releasing 5'-nucleotide monophosphates. In prokaryotes, RNase II and RNase R have two N-terminal CSD and one C-terminal S1 domain involved in RNA binding, and a central catalytic RNB domain. In eukaryotes, Rrp44p/Dis3, is a RNase II-like protein with similar modular organization, that is the only catalytically active nuclease in the exosome, a complex crucial for RNA metabolism. Here we review recent progresses in the understanding of the degradation mechanism of RNase II, based on mutational analysis and their characterization regarding catalysis and RNA affinity. We have given particular emphasis on E. coli RNase II but the synergies between the functional and structural studies have shown that our findings have implications in the understanding the similar mode of action of other RNase II family members.