Phosphoproteomic Analysis Reveals Rio1-Related Protein Phosphorylation Changes in Response to UV Irradiation in Sulfolobus islandicus REY15A.

Phosphoproteomic Analysis Reveals Rio1-Related Protein Phosphorylation Changes in Response to UV Irradiation in Sulfolobus islandicus REY15A.
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磷酸蛋白质组学分析揭示了岛硫化叶菌 REY15A 中 Rio1 相关蛋白对紫外线照射的磷酸化变化

DOI:
10.3389/fmicb.2020.586025
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发表时间:
2020
影响因子:
5.2
通讯作者:
Shen Y
Shen Y
中科院分区:
生物学2区
文献类型:
--
作者:
Huang Q;Lin Z;Wu P;Ni J;Shen Y

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真核生物的DNA损伤反应(DDR)在很大程度上受蛋白质磷酸化的调节。在古细菌中,许多蛋白质被磷酸化,然而,目前还不清楚细胞如何通过整体蛋白质磷酸化来响应DNA损伤。我们以前发现,Δ rio 1,一个Rio 1激酶同源物缺失菌株的硫化叶菌REY 15 A,是敏感的紫外线照射。在这项研究中,我们发现Δ rio 1比野生型生长得更快。对野生型和Δ rio 1进行定量磷酸化蛋白质组学分析,发现在333个蛋白质中总共有562个磷酸化位点(Ser/Thr/Tyr比率为65.3%/23.8%/10.9%)。在紫外光照射下,野生型菌株中有30个蛋白质的35个位点的磷酸化水平发生了>1.3倍的变化。有趣的是,野生型中超过一半的UV诱导的变化没有发生在Δ rio 1菌株中,这些变化主要与蛋白质合成和周转有关。此外,蛋白激酶和几个转录调控差异磷酸化后,UV处理,和一些变化依赖于Rio 1。最后,许多参与各种细胞代谢的蛋白质表现出Riol相关的和UV无关的磷酸化变化。我们的研究结果表明,Rio 1参与调节蛋白质回收和信号转导响应紫外线照射,并在多个细胞过程中发挥调节作用,在S。冰岛人。
DNA damage response (DDR) in eukaryotes is largely regulated by protein phosphorylation. In archaea, many proteins are phosphorylated, however, it is unclear how the cells respond to DNA damage through global protein phosphorylation. We previously found that Δrio1, a Rio1 kinase homolog deletion strain of Sulfolobus islandicus REY15A, was sensitive to UV irradiation. In this study, we showed that Δrio1 grew faster than the wild type. Quantitative phosphoproteomic analysis of the wild type and Δrio1, untreated and irradiated with UV irradiation, revealed 562 phosphorylated sites (with a Ser/Thr/Tyr ratio of 65.3%/23.8%/10.9%) of 333 proteins in total. The phosphorylation levels of 35 sites of 30 proteins changed with >1.3-fold in the wild type strain upon UV irradiation. Interestingly, more than half of the UV-induced changes in the wild type did not occur in the Δrio1 strain, which were mainly associated with proteins synthesis and turnover. In addition, a protein kinase and several transcriptional regulators were differentially phosphorylated after UV treatment, and some of the changes were dependent on Rio1. Finally, many proteins involved in various cellular metabolisms exhibited Riol-related and UV-independent phosphorylation changes. Our results suggest that Rio1 is involved in the regulation of protein recycling and signal transduction in response to UV irradiation, and plays regulatory roles in multiple cellular processes in S. islandicus.
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