2'-5'-oligoadenylate 合成酶不同的结构域和多样性。

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS
ACS Applied Bio Materials Pub Date : 2024-08-01 Epub Date: 2024-04-11 DOI:10.1139/bcb-2023-0369
Amit Koul, Lok Tin Hui, Nikhat Lubna, Sean A McKenna
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引用次数: 0

摘要

2'-5'寡聚腺苷酸合成酶(OAS)是先天性免疫系统的重要组成部分,能识别病毒双链 RNA(dsRNA)。与 dsRNA 结合后,OAS 生成 2'-5'-linked oligoadenylates(2-5A),激活核糖核酸酶 L(RNase L),阻止病毒复制。因此,OAS/RNase L 途径是一条重要的抗病毒途径,病毒已设计出规避 OAS 激活的策略。OAS 酶按大小分为四类:小型(OAS1)、中型(OAS2)和大型(OAS3),分别由一个、两个和三个 OAS 结构域组成;OAS 类蛋白(OASL)由一个 OAS 结构域和类似泛素的串联结构域组成。早期对 OAS 酶的研究提示了 OAS 对 dsRNA 的识别,但由于 OAS 家族成员的大小不同,再加上缺乏全长 OAS2 和 OAS3 的结构信息,人们对 dsRNA 对 OAS 催化活性的调控并不十分清楚。然而,最近对 OAS 的生物物理研究突出了其整体结构和结构域组织。在这篇综述中,我们详细考察了 OAS 的文献,并总结了对 2' 5'-oligoadenylate 合成酶的研究。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Distinct domain organization and diversity of 2'-5'-oligoadenylate synthetases.

The 2'-5'-oligoadenylate synthetases (OAS) are important components of the innate immune system that recognize viral double-stranded RNA (dsRNA). Upon dsRNA binding, OAS generate 2'-5'-linked oligoadenylates (2-5A) that activate ribonuclease L (RNase L), halting viral replication. The OAS/RNase L pathway is thus an important antiviral pathway and viruses have devised strategies to circumvent OAS activation. OAS enzymes are divided into four classes according to size: small (OAS1), medium (OAS2), and large (OAS3) that consist of one, two, and three OAS domains, respectively, and the OAS-like protein (OASL) that consists of one OAS domain and tandem domains similar to ubiquitin. Early investigation of the OAS enzymes hinted at the recognition of dsRNA by OAS, but due to size differences amongst OAS family members combined with the lack of structural information on full-length OAS2 and OAS3, the regulation of OAS catalytic activity by dsRNA was not well understood. However, the recent biophysical studies of OAS have highlighted overall structure and domain organization. In this review, we present a detailed examination of the OAS literature and summarized the investigation on 2'-5'-oligoadenylate synthetases.

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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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