The protein-only RNase Ps, endonucleases that cleave pre-tRNA: Biological relevance, molecular architectures, substrate recognition and specificity, and protein interactomes.

IF 6.4 2区 生物学 Q1 CELL BIOLOGY
Catherine A Wilhelm, Kipchumba Kaitany, Abigail Kelly, Matthew Yacoub, Markos Koutmos
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引用次数: 0

Abstract

Protein-only RNase P (PRORP) is an essential enzyme responsible for the 5' maturation of precursor tRNAs (pre-tRNAs). PRORPs are classified into three categories with unique molecular architectures, although all three classes of PRORPs share a mechanism and have similar active sites. Single subunit PRORPs, like those found in plants, have multiple isoforms with different localizations, substrate specificities, and temperature sensitivities. Most recently, Arabidopsis thaliana PRORP2 was shown to interact with TRM1A and B, highlighting a new potential role between these enzymes. Work with At PRORPs led to the development of a ribonuclease that is being used to protect against plant viruses. The mitochondrial RNase P complex, found in metazoans, consists of PRORP, TRMT10C, and SDR5C1, and has also been shown to have substrate specificity, although the cause is unknown. Mutations in mitochondrial tRNA and mitochondrial RNase P have been linked to human disease, highlighting the need to continue understanding this complex. The last class of PRORPs, homologs of Aquifex RNase P (HARPs), is found in thermophilic archaea and bacteria. This most recently discovered type of PRORP forms a large homo-oligomer complex. Although numerous structures of HARPs have been published, it is still unclear how HARPs bind pre-tRNAs and in what ratio. There is also little investigation into the substrate specificity and ideal conditions for HARPs. Moving forward, further work is required to fully characterize each of the three classes of PRORP, the pre-tRNA binding recognition mechanism, the rules of substrate specificity, and how these three distinct classes of PRORP evolved. This article is categorized under: RNA Structure and Dynamics > RNA Structure, Dynamics and Chemistry RNA Structure and Dynamics > Influence of RNA Structure in Biological Systems.

只含蛋白质的 RNase Ps,可裂解前 tRNA 的内切核酸酶:生物学相关性、分子结构、底物识别和特异性以及蛋白质相互作用组。
纯蛋白 RNase P(PRORP)是一种负责前体 tRNA(前 tRNA)5'成熟的重要酶。PRORPs 可分为三类,具有独特的分子结构,但所有三类 PRORPs 都具有相同的机制和相似的活性位点。单亚基 PRORPs(如植物中发现的 PRORPs)有多种异构体,其定位、底物特异性和温度敏感性各不相同。最近,拟南芥 PRORP2 与 TRM1A 和 TRM1B 相互作用,突显了这些酶之间新的潜在作用。通过研究拟南芥 PRORPs,开发出了一种核糖核酸酶,这种酶被用于抵御植物病毒。线粒体 RNase P 复合物存在于变态类动物中,由 PRORP、TRMT10C 和 SDR5C1 组成,也被证明具有底物特异性,但原因不明。线粒体 tRNA 和线粒体 RNase P 的突变与人类疾病有关,因此有必要继续了解这一复合体。最后一类 PRORPs,即 Aquifex RNase P 的同源物(HARPs),存在于嗜热古细菌和细菌中。这种最新发现的 PRORP 形成了一个大型同源异构体复合物。虽然已经公布了许多 HARPs 的结构,但仍不清楚 HARPs 如何结合前 tRNA 以及结合的比例。对 HARPs 的底物特异性和理想条件的研究也很少。展望未来,还需要进一步研究这三类 PRORP 的特性、前 tRNA 结合识别机制、底物特异性规则以及这三类不同的 PRORP 是如何进化的。本文归类于RNA 结构与动力学 > RNA 结构、动力学与化学 RNA 结构与动力学 > RNA 结构在生物系统中的影响。
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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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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