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ANGUSTIFOLIA a Plant Homolog of CtBP/BARS Localizes to Stress Granules and Regulates Their Formation

机译:CtBP / BARS的植物同源物ANGUSTIFOLIA定位于应力颗粒并调节其形成

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摘要

The ANGUSTIFOLIA (AN) gene in Arabidopsis is important for a plethora of morphological phenotypes. Recently, AN was also reported to be involved in responses to biotic and abiotic stresses. It encodes a homolog of the animal C-terminal binding proteins (CtBPs). In contrast to animal CtBPs, AN does not appear to function as a transcriptional co-repressor and instead functions outside nucleus where it might be involved in Golgi-associated membrane trafficking. In this study, we report a novel and unexplored role of AN as a component of stress granules (SGs). Interaction studies identified several RNA binding proteins that are associated with AN. AN co-localizes with several messenger ribonucleoprotein granule markers to SGs in a stress dependent manner. an mutants exhibit an altered SG formation. We provide evidence that the NAD(H) binding domain of AN is relevant in this context as proteins carrying mutations in this domain localize to a much higher degree to SGs and strongly reduce AN dimerization and its interaction with one interactor but not the others. Finally, we show that AN is a negative regulator of salt and osmotic stress responses in Arabidopsis suggesting a functional relevance in SGs.
机译:拟南芥中的ANGUSTIFOLIA(AN)基因对于过多的形态表型非常重要。最近,据报道AN也参与对生物和非生物胁迫的反应。它编码动物C末端结合蛋白(CtBPs)的同源物。与动物CtBP相比,AN似乎不起转录共阻遏物的作用,而是在细胞核外起作用,可能与高尔基体相关的膜运输有关。在这项研究中,我们报告了AN作为应力颗粒(SGs​​)的组成部分的一种新型且尚未探索的作用。相互作用研究确定了几种与AN相关的RNA结合蛋白。 AN与几种信使核糖核蛋白颗粒标记物以应力依赖性方式共定位于SG。突变体表现出改变的SG形成。我们提供的证据表明,AN的NAD(H)结合结构域在此情况下是相关的,因为在该结构域中携带突变的蛋白质在很大程度上定位于SG,并强烈减少了AN二聚化及其与一种相互作用因子的相互作用,而与其他相互作用因子没有相互作用。最后,我们表明AN是拟南芥中盐和渗透胁迫反应的负调节剂,提示SGs具有功能相关性。

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