Protein kinase ATR inhibits E3 ubiquitin ligase CRL4(PRL1) to stabilize ribonucleotide reductase in response to replication stress
文献类型： 外文期刊
第一作者： Bao, Weiyi
作者： Bao, Weiyi;Zhang, Weijia;Huang, Yongchi;Zhao, Yan;Duan, Leilei;Wang, Lili;Yan, Shunping;Bao, Weiyi;Zhang, Weijia;Huang, Yongchi;Zhao, Yan;Duan, Leilei;Wang, Lili;Yan, Shunping;Bao, Weiyi;Zhang, Weijia;Huang, Yongchi;Zhao, Yan;Duan, Leilei;Wang, Lili;Yan, Shunping;Bao, Weiyi;Zhang, Weijia;Huang, Yongchi;Zhao, Yan;Duan, Leilei;Wang, Lili;Yan, Shunping;Bao, Weiyi;Zhang, Weijia;Huang, Yongchi;Zhao, Yan;Duan, Leilei;Wang, Lili;Yan, Shunping
作者机构：
期刊名称：CELL REPORTS （ 影响因子：8.8； 五年影响因子：9.9 ）
ISSN： 2211-1247
年卷期： 2023 年 42 卷 7 期
页码：
收录情况： SCI
摘要： The protein kinase ATR is essential for replication stress responses in all eukaryotes. Ribonucleotide reductase (RNR) catalyzes the formation of deoxyribonucleotide (dNTP), the universal building block for DNA replication and repair. However, the relationship between ATR and RNR is not well understood. Here, we show that ATR promotes the protein stability of RNR in Arabidopsis. Through an activation tagging-based genetic screen, we found that overexpression of TSO2, a small subunit of RNR, partially suppresses the hypersensitivity of the atr mutant to replication stress. Biochemically, TSO2 interacts with PRL1, a central subunit of the Cullin4-based E3 ubiquitin ligase CRL4(PRL1), which polyubiquitinates TSO2 and promotes its degradation. ATR inhibits CRL4(PRL1) to attenuate TSO2 degradation. Our work provides an important insight into the replication stress responses and a post-translational regulatory mechanism for RNR. Given the evolutionary conservation of the proteins involved, the ATR-PRL1-RNR module may act across eukaryotes.
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