The protein phosphatase PC1 dephosphorylates and deactivates CatC to negatively regulate H2O2 homeostasis and salt tolerance in rice
文献类型： 外文期刊
作者： Liu, Cong 1 ; Lin, Jian-Zhong 1 ; Wang, Yan 1 ; Tian, Ye 1 ; Zheng, He-Ping 1 ; Zhou, Zheng-Kun 1 ; Zhou, Yan-Biao 2 ; Tang, Xiao-Dan 2 ; Zhao, Xin-Hui 2 ; Wu, Ting 1 ; Xu, Shi-Long 2 ; Tang, Dong-Ying 1 ; Zuo, Ze-Cheng 3 ; He, Hang 4 ; Bai, Lian-Yang 6 ; Yang, Yuan-Zhu 2 ; Liu, Xuan-Ming 1 ;
作者机构： 1.Hunan Univ, Natl Ctr Technol Innovat Saline Alkali Tolerant Ri, Hunan Prov Key Lab Plant Funct Genom & Dev Regulat, Coll Biol,State Key Lab Chemo Biosensing & Chemome, Changsha 410082, Peoples R China
2.Yuan Longping High Tech Agr Co Ltd, Minist Agr & Rural Affairs, Key Lab Southern Rice Innovat & Improvement, Hunan Engn Lab Dis & Pest Resistant Rice Breeding, Changsha 410001, Peoples R China
3.Jilin Univ, Coll Plant Sci, Jilin Prov Engn Lab Plant Genet Improvement, Changchun 130062, Peoples R China
4.Peking Univ, Sch Adv Agr Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China
5.Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China
6.Hunan Acad Agr Sci, Hunan Agr Biotechnol Res Inst, Changsha 410125, Peoples R China
期刊名称：PLANT CELL （ 影响因子：11.6； 五年影响因子：12.9 ）
ISSN： 1040-4651
年卷期： 2023 年
页码：
收录情况： SCI
摘要： A protein phosphatase, PC1, specifically dephosphorylates Catalase C at Ser-9 to accelerate the disassociation of its tetramer to negatively regulate H2O2 homeostasis in rice. Catalase (CAT) is often phosphorylated and activated by protein kinases to maintain hydrogen peroxide (H2O2) homeostasis and protect cells against stresses, but whether and how CAT is switched off by protein phosphatases remains inconclusive. Here, we identified a manganese (Mn2+)-dependent protein phosphatase, which we named PHOSPHATASE OF CATALASE 1 (PC1), from rice (Oryza sativa L.) that negatively regulates salt and oxidative stress tolerance. PC1 specifically dephosphorylates CatC at Ser-9 to inhibit its tetramerization and thus activity in the peroxisome. PC1 overexpressing lines exhibited hypersensitivity to salt and oxidative stresses with a lower phospho-serine level of CATs. Phosphatase activity and seminal root growth assays indicated that PC1 promotes growth and plays a vital role during the transition from salt stress to normal growth conditions. Our findings demonstrate that PC1 acts as a molecular switch to dephosphorylate and deactivate CatC and negatively regulate H2O2 homeostasis and salt tolerance in rice. Moreover, knockout of PC1 not only improved H2O2-scavenging capacity and salt tolerance but also limited rice grain yield loss under salt stress conditions. Together, these results shed light on the mechanisms that switch off CAT and provide a strategy for breeding highly salt-tolerant rice.
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