Ribonuclease III mechanisms of double-stranded RNA cleavage.
Ribonuclease III mechanisms of double-stranded RNA cleavage.
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DOI：
10.1002/wrna.1195
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发表时间：
2014-01
影响因子：
7.3
通讯作者：
Nicholson, Allen W.
中科院分区：
文献类型：
--
作者：
Nicholson, Allen W.
双链RNA在细菌和真核细胞的基因表达和调控、宿主防御和基因组监视中具有不同的作用。dsRNA功能的一个中心方面是其被二价金属离子依赖性磷酸二酯酶的核糖核酸酶III（RNase III）家族的成员选择性识别和切割。RNA酶III家族成员对dsRNA的加工是编码和非编码RNA（包括miRNA和siRNA）成熟和衰变的重要步骤。核糖核酸酶III，作为第一个纯化的大肠杆菌，已作为一个生物化学特征良好的原型，和其他细菌直系同源物提供了第一个结构信息。RNase III家族成员共有一个独特的折叠（RNase III结构域），可以二聚化形成结合dsRNA并切割每条链上的磷酸二酯的结构，提供特征性的2 nt，3′-突出端产物末端。正在进行的研究正在揭示其他结构域的功能，包括与RNase III结构域合作以选择靶位点、调节活性、赋予持续合成能力并支持识别结构多样的底物的dsRNA结合和PAZ结构域。RNase III酶在由不同输入调节的多组分组装中起作用，并且至少一种RNase III相关多肽可以作为非催化的dsRNA结合蛋白发挥作用。本文综述了RNase III家族成员的催化和靶位点选择机制的现有知识，并讨论了这些酶及其与dsRNA相互作用的不太清楚的方面。WIREs RNA 2014，5：31-48。doi：10.1002/wrna.1195
Double-stranded(ds) RNA has diverse roles in gene expression and regulation, host defense, and genome surveillance in bacterial and eukaryotic cells. A central aspect of dsRNA function is its selective recognition and cleavage by members of the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. The processing of dsRNA by RNase III family members is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs. RNase III, as first purified from Escherichia coli, has served as a biochemically well-characterized prototype, and other bacterial orthologs provided the first structural information. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3′-overhang product ends. Ongoing studies are uncovering the functions of additional domains, including, inter alia, the dsRNA-binding and PAZ domains that cooperate with the RNase III domain to select target sites, regulate activity, confer processivity, and support the recognition of structurally diverse substrates. RNase III enzymes function in multicomponent assemblies that are regulated by diverse inputs, and at least one RNase III-related polypeptide can function as a noncatalytic, dsRNA-binding protein. This review summarizes the current knowledge of the mechanisms of catalysis and target site selection of RNase III family members, and also addresses less well understood aspects of these enzymes and their interactions with dsRNA. WIREs RNA 2014, 5:31–48. doi: 10.1002/wrna.1195
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