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首页> 外文期刊>Cell Division >Replication stress-induced Exo1 phosphorylation is mediated by Rad53/Pph3 and Exo1 nuclear localization is controlled by 14-3-3 proteins
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Replication stress-induced Exo1 phosphorylation is mediated by Rad53/Pph3 and Exo1 nuclear localization is controlled by 14-3-3 proteins

机译：复制应激诱导的Exo1磷酸化是由Rad53 / Pph3介导的，并且Exo1的核定位是由14-3-3蛋白控制的

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Mechanisms controlling DNA resection at sites of damage and affecting genome stability have been the subject of deep investigation, though their complexity is not yet fully understood. Specifically, the regulatory role of post-translational modifications in the localization, stability and function of DNA repair proteins is an important aspect of such complexity. Here, we took advantage of the superior resolution of phosphorylated proteins provided by Phos-Tag technology to study pathways controlling the reversible phosphorylation of yeast Exo1, an exonuclease involved in a number of DNA repair pathways. We report that Rad53, a checkpoint kinase downstream of Mec1, is responsible for Exo1 phosphorylation in response to DNA replication stress and we demonstrate a role for the type-2A protein phosphatase Pph3 in the dephosphorylation of both Rad53 and Exo1 during checkpoint recovery. Fluorescence microscopy studies showed that Rad53-dependent phosphorylation is not required for the recruitment or the release of Exo1 from the nucleus, whereas 14-3-3 proteins are necessary for Exo1 nuclear translocation. By shedding light on the mechanism of Exo1 control, these data underscore the importance of post-translational modifications and protein interactions in the regulation of DNA end resection.
机译：尽管尚不完全了解其复杂性，但控制损伤部位DNA切除并影响基因组稳定性的机制一直是深入研究的主题。特别地，翻译后修饰在DNA修复蛋白的定位，稳定性和功能中的调节作用是这种复杂性的重要方面。在这里，我们利用了Phos-Tag技术提供的磷酸化蛋白质的高分离度来研究控制酵母Exo1（一种参与许多DNA修复途径的核酸外切酶）可逆磷酸化的途径。我们报告说Rad53，Mec1的下游检查点激酶，负责响应DNA复制压​​力的Exo1磷酸化，并且我们证明了2A型蛋白磷酸酶Pph3在检查点恢复期间Rad53和Exo1的去磷酸化中的作用。荧光显微镜研究表明，从核中募集或释放Exo1不需要Rad53依赖的磷酸化，而14-3-3蛋白对于Exo1核转运是必需的。通过阐明Exo1控制机制，这些数据强调了翻译后修饰和蛋白质相互作用在调节DNA末端切除中的重要性。

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