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首页> 外文期刊>Journal of Molecular Biology >TRIM25 Binds RNA to Modulate Cellular Anti-viral Defense
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TRIM25 Binds RNA to Modulate Cellular Anti-viral Defense

机译：Trim25结合RNA调节细胞抗病毒防御

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摘要

TRIM25 is a multi-domain, RING-type E3 ubiquitin ligase of the tripartite motif family that has important roles in multiple RNA-dependent processes. In particular, TRIM25 functions as an effector of RIG-I and ZAP, which are innate immune sensors that recognize viral RNA and induce ubiquitin-dependent anti-viral response mechanisms. TRIM25 is reported to also bind RNA, but the molecular details of this interaction or its relevance to anti-viral defense have not been elucidated. Here, we characterize the RNA-binding activity of TRIM25 and find that the protein binds both single-stranded and double-stranded RNA. Multiple regions of TRIM25 contribute to this functionality, including the C-terminal SPRY domain and a lysine-rich motif in the linker segment connecting the SPRY and coiled-coil domains. RNA binding modulates TRIM25's ubiquitination activity in vitro, its localization in cells, and its anti-viral activity. Taken together with other studies, our results indicate that RNA binding by TRIM25 has at least three important functional consequences: by enhancing ubiquitination activity, either through allosteric effects or through clustering of multiple TRIM25 molecules; by modulating the multi-domain structure of the TRIM25 dimer, and thereby structural coupling of the SPRY and RBCC elements during the ubiquitination reaction; and by facilitating subcellular localization of the E3 ligase during virus infection. (C) 2018 Elsevier Ltd. All rights reserved.
机译：Trim25是三方依赖过程中具有重要作用的三方基质系列的多域，环型E3泛素连接酶。特别地，Trim25用作钻机I和ZAP的效应器，这是识别病毒RNA并诱导泛素依赖性抗病毒反应机制的先天免疫传感器。据报道Trim25还涉及该rNA，但是这种相互作用的分子细节或其与抗病毒防御的相关性尚未得到阐明。这里，我们表征Trim25的RNA结合活性，并发现蛋白质结合单链和双链RNA。修剪25的多个区域有助于该功能，包括C末端SPry结构域和连接Spry和卷绕线圈结构域的接头段中的富赖氨酸的基序。 RNA结合在体外调节Trim25的泛素化活性，其在细胞中的本地化及其抗病毒活性。与其他研究一起携带，我们的结果表明Trim25的RNA结合具有至少三种重要的功能后果：通过增强泛素化活性，通过颠覆效果或通过多个TRIM25分子的聚类;通过调节Trim25二聚体的多域结构，从而在泛素化反应期间的Spry和RBCC元件的结构耦合;并通过在病毒感染期间促进E3连接酶的亚细胞定位。 （c）2018年elestvier有限公司保留所有权利。

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