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.

真核生物中的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，但是，不清楚细胞如何通过整体蛋白质磷酸化来应对DNA损伤。我们先前发现Δ里奥1，是Rio1激酶同源缺失菌株 海岛REY15A对紫外线辐射敏感。在这项研究中，我们表明里奥1比野生型增长更快。野生型和Δ的磷酸化蛋白质组学定量分析里奥1，未经处理并用紫外线辐射，显示总共333种蛋白质的562个磷酸化位点（Ser / Thr / Tyr比为65.3％/ 23.8％/ 10.9％）。在紫外线照射下，野生型菌株中30种蛋白质的35个位点的磷酸化水平变化> 1.3倍。有趣的是，紫外线引起的野生型变化的一半以上没有发生在Δ中里奥1菌株，主要与蛋白质合成和周转有关。此外，紫外线处理后，一个蛋白激酶和几个转录调节子被差异磷酸化，其中一些变化取决于Rio1。最后，参与各种细胞代谢的许多蛋白质表现出与Riol相关和与UV无关的磷酸化变化。我们的结果表明，Rio1参与了蛋白质回收和信号转导的调控，以响应紫外线辐射，并在多种细胞过程中起调控作用。S. islandicus。