RNase P 在前体 tRNA 处理过程中的多种结构。

IF 6.4 2区 生物学 Q1 CELL BIOLOGY Wiley Interdisciplinary Reviews: RNA Pub Date : 2024-03-01 DOI:10.1002/wrna.1835
Sagar Sridhara
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引用次数: 0

摘要

前体转移 RNA(pre-tRNA)需要经过大量加工才能生成成熟的 tRNA,这些 tRNA 具有适当的折叠、结构稳定性和维持细胞活力所需的功能。tRNA 的成熟过程是有序的:5'-加工、3'-加工、特定位点修饰(如果有的话)、3'-CCA 添加,然后进行氨基酰化并加入细胞蛋白质合成机制。核糖核酸酶 P(RNase P)是所有生命领域中普遍保留的核酸内切酶,通过去除核苷酸-1 位和+1 位之间的磷酸二酯连接,在 5'端水解前 tRNA 序列。除了一种古生物RNase P 是生命中不可或缺的酶,在酶亚基组成、底物识别机制和活性位点结构等方面都有基本的差异,但在所有情况下都利用两种金属离子介导的保守催化反应。众所周知,细菌、古生物和真核生物中都存在典型的基于 RNA 的核糖核蛋白 RNase P,但最近发现真核生物中存在不含 RNA 的纯蛋白 RNase P,原核生物中也存在不含 RNA 的 Aquifex RNase P 同源物。本综述旨在全面概述各种基于 RNA 和不含 RNA 的 RNase P 全酶在实现保守的前 tRNA 处理功能过程中利用关键的 RNA 蛋白和蛋白蛋白相互作用所表现出的结构多样性。此外,文章还结合 RNase P 在一些临床和生物技术应用中的适用性,讨论了 RNase P 的替代作用和功能互换性。本文归类于RNA 处理 > tRNA 处理 RNA 进化和基因组学 > RNA 和核糖核蛋白进化 RNA 与蛋白质和其他分子的相互作用 > RNA 蛋白复合物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Multiple structural flavors of RNase P in precursor tRNA processing.

The precursor transfer RNAs (pre-tRNAs) require extensive processing to generate mature tRNAs possessing proper fold, structural stability, and functionality required to sustain cellular viability. The road to tRNA maturation follows an ordered process: 5'-processing, 3'-processing, modifications at specific sites, if any, and 3'-CCA addition before aminoacylation and recruitment to the cellular protein synthesis machinery. Ribonuclease P (RNase P) is a universally conserved endonuclease in all domains of life, performing the hydrolysis of pre-tRNA sequences at the 5' end by the removal of phosphodiester linkages between nucleotides at position -1 and +1. Except for an archaeal species: Nanoarchaeum equitans where tRNAs are transcribed from leaderless-position +1, RNase P is indispensable for life and displays fundamental variations in terms of enzyme subunit composition, mechanism of substrate recognition and active site architecture, utilizing in all cases a two metal ion-mediated conserved catalytic reaction. While the canonical RNA-based ribonucleoprotein RNase P has been well-known to occur in bacteria, archaea, and eukaryotes, the occurrence of RNA-free protein-only RNase P in eukaryotes and RNA-free homologs of Aquifex RNase P in prokaryotes has been discovered more recently. This review aims to provide a comprehensive overview of structural diversity displayed by various RNA-based and RNA-free RNase P holoenzymes towards harnessing critical RNA-protein and protein-protein interactions in achieving conserved pre-tRNA processing functionality. Furthermore, alternate roles and functional interchangeability of RNase P are discussed in the context of its employability in several clinical and biotechnological applications. This article is categorized under: RNA Processing > tRNA Processing RNA Evolution and Genomics > RNA and Ribonucleoprotein Evolution RNA Interactions with Proteins and Other Molecules > RNA-Protein Complexes.

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来源期刊
CiteScore
14.80
自引率
4.10%
发文量
67
审稿时长
6-12 weeks
期刊介绍: WIREs RNA aims to provide comprehensive, up-to-date, and coherent coverage of this interesting and growing field, providing a framework for both RNA experts and interdisciplinary researchers to not only gain perspective in areas of RNA biology, but to generate new insights and applications as well. Major topics to be covered are: RNA Structure and Dynamics; RNA Evolution and Genomics; RNA-Based Catalysis; RNA Interactions with Proteins and Other Molecules; Translation; RNA Processing; RNA Export/Localization; RNA Turnover and Surveillance; Regulatory RNAs/RNAi/Riboswitches; RNA in Disease and Development; and RNA Methods.
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