Microbiology and Infectiology Department, University of Sherbrooke, Sherbrooke, Quebec, Canada.
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, Maryland.
Wiley Interdiscip Rev RNA. 2019 May;10(3):e1521. doi: 10.1002/wrna.1521. Epub 2018 Dec 11.
The double-stranded RNA-binding protein (dsRBP) family controls RNA editing, stability, and function in all eukaryotes. The central feature of this family is the recognition of a generic RNA duplex using highly conserved double-stranded RNA-binding domain (dsRBD) that recognizes the characteristic distance between the minor grooves created by the RNA helix. Variations on this theme that confer species and functional specificities have been reported but most dsRBPs retain their capacity to bind generic dsRNA. The ribonuclease III (RNase III) family members fall into four classes, represented by bacterial RNase III, yeast Rnt1p, human Drosha, and human Dicer, respectively. Like all dsRBPs and most members of the RNase III family, Rnt1p has a dsRBD, but unlike most of its kin, it poorly binds to generic RNA helices. Instead, Rnt1p, the only known RNase III expressed in Saccharomyces cerevisiae that lacks the RNAi (RNA interference) machinery, recognizes a specific class of stem-loop structures. To recognize the specific substrates, the dsRBD of Rnt1p is specialized, featuring a αβββααα topology and a sequence-specific RNA-binding motif at the C-terminus. Since the discovery of Rnt1p in 1996, significant progress has been made in studies of its genetics, function, structure, and mechanism of action, explaining the reasons and mechanisms for the increased specificity of this enzyme and its impact on the mechanism of RNA degradation. This article is categorized under: RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms RNA Interactions with Proteins and Other Molecules > Protein-RNA Recognition RNA Processing > Processing of Small RNAs RNA Interactions with Proteins and Other Molecules > RNA-Protein Complexes.
双链 RNA 结合蛋白（dsRBP）家族控制所有真核生物中 RNA 的编辑、稳定性和功能。该家族的核心特征是使用高度保守的双链 RNA 结合域（dsRBD）识别通用的 RNA 双链，该结构域识别由 RNA 螺旋形成的小沟之间的特征距离。已经报道了具有物种和功能特异性的这种主题的变体，但大多数 dsRBPs 保留其结合通用 dsRNA 的能力。核糖核酸酶 III（RNase III）家族成员分为四类，分别由细菌 RNase III、酵母 Rnt1p、人 Drosha 和人 Dicer 代表。与所有 dsRBPs 和大多数 RNase III 家族成员一样，Rnt1p 具有 dsRBD，但与大多数同类蛋白不同，它与通用 RNA 螺旋的结合能力较差。相反，Rnt1p 是酵母 Saccharomyces cerevisiae 中唯一已知的缺乏 RNAi（RNA 干扰）机制的 RNase III，它识别特定的茎环结构类。为了识别特定的底物，Rnt1p 的 dsRBD 具有专业化的特征，具有 αβββααα 拓扑结构和 C 末端的序列特异性 RNA 结合基序。自 1996 年发现 Rnt1p 以来，在其遗传学、功能、结构和作用机制的研究方面取得了重大进展，解释了该酶特异性增加的原因和机制及其对 RNA 降解机制的影响。本文归类于：RNA 周转和监测 > 周转/监测机制 RNA 与蛋白质和其他分子的相互作用 > 蛋白质-RNA 识别 RNA 加工 > 小 RNA 的加工 RNA 与蛋白质和其他分子的相互作用 > RNA-蛋白质复合物。
