摘要
原核和真核RNA的 3′末端可被聚腺苷酸化,且已知聚腺苷酸化的作用是增加真核转录的稳定性,而促进原核转录的不稳定性。RNA被认为是毒力机制的重要效应器,因其直接参与致病菌的调节途径。因此RNA的脱腺苷化是一个重要控制点和成功的限速步骤。核糖核酸酶(RNase AS)是结核分枝杆菌一种新型的识别蛋白,它极大妨碍了体内分枝杆菌的毒力,其机制仍有待全面确定。系统分类鉴定了所有分枝杆菌中RNase AS的直系同源性。然而,最近的功能数据仅阐明了RNase AS是一种高度特异性降解RNA聚腺苷酸化序列的核糖核酸酶外切酶。本文综述了RNase AS的结构和功能的目前知识,强调了其在RNA成熟进程中的作用。所有分枝杆菌核糖核酸酶迄今为止的特征的总体描述也被提供。
关键词: 功能,核糖核酸酶,结构,肺结核
Current Medicinal Chemistry
Title:Structure and Function of RNase AS: A Novel Virulence Factor From Mycobacterium tuberculosis
Volume: 22 Issue: 14
Author(s): Maria Romano, Flavia Squeglia and Rita Berisio
Affiliation:
关键词: 功能,核糖核酸酶,结构,肺结核
摘要: The 3′-ends of both prokaryotic and eukaryotic RNA can be polyadenylated and the effect of polyadenylation is known to increase the stability of transcripts in eukaryotes, whereas it promotes instability in prokaryotes. RNAs are considered as key effectors of virulence mechanisms, since they are directly involved in regulatory pathways in pathogenic bacteria. Deadenylation of RNA is thus an important control point and rate-limiting step of its turnover. RNase AS is a novel identified protein of Mycobacterium tuberculosis, which dramatically hampers mycobacterial virulence in vivo, with a mechanism which is still to be fully defined. Phylogenetic analysis identifies orthologs of RNase AS in all mycobacteria. However, functional data only recently clarified that RNase AS is an exo-ribonuclease, which is highly specific in degrading polyadenylate sequences of RNA. This Review summarizes the current knowledge on structure and function of RNase AS and underscores its role in the process of RNA maturation. An overall description of all mycobacterial ribonucleases hitherto characterized is also provided.
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Cite this article as:
Maria Romano, Flavia Squeglia and Rita Berisio , Structure and Function of RNase AS: A Novel Virulence Factor From Mycobacterium tuberculosis, Current Medicinal Chemistry 2015; 22 (14) . https://dx.doi.org/10.2174/0929867322666150417125301
DOI https://dx.doi.org/10.2174/0929867322666150417125301 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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