J Integr Plant Biol ›› 2022, Vol. 64 ›› Issue (5): 1087-1101.DOI: 10.1111/jipb.13255

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  • 收稿日期:2022-01-19 接受日期:2022-03-27 出版日期:2022-05-01 发布日期:2022-05-19

OsDMI3-mediated OsUXS3 phosphorylation improves oxidative stress tolerance by modulating OsCATB protein abundance in rice

Lan Ni1†, Qingwen Wang1†, Chao Chen1, Shuang Wang1, Tao Shen1, Jingjing Jiang1, Zhenzhen Cui1, Kaiyue Li1, Qiqing Yang1 and Mingyi Jiang1,2*   

  1. 1 College of Life Sciences, National Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Crop Physiology Ecology and Production Management, Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, China
    2 Southern Regional Collaborative Innovation Center for Grain and Oil Crops in China, Hunan Agricultural University, Changsha 410128, China

    These authors contributed equally to this work.
    *Correspondence: Mingyi Jiang (myjiang@njau.edu.cn)
  • Received:2022-01-19 Accepted:2022-03-27 Online:2022-05-01 Published:2022-05-19

Abstract:

Calcium (Ca2+)/calmodulin (CaM)-dependent protein kinase (CCaMK) is an important positive regulator of antioxidant defenses and tolerance against oxidative stress. However, the underlying molecular mechanisms are largely unknown. Here, we report that the rice (Oryza sativa) CCaMK (OsDMI3) physically interacts with and phosphorylates OsUXS3, a cytosol-localized UDP-xylose synthase. Genetic and biochemical evidence demonstrated that OsUXS3 acts downstream of OsDMI3 to enhance the oxidative stress tolerance conferred by higher catalase (CAT) activity. Indeed, OsUXS3 interacted with CAT isozyme B (OsCATB), and this interaction was required to increase OsCATB protein abundance under oxidative stress conditions. Furthermore, we showed that OsDMI3 phosphorylates OsUXS3 on residue Ser-245, thereby further promoting the interaction between OsUXS3 and OsCATB. Our results indicate that OsDMI3 promotes the association of OsUXS3 with OsCATB to enhance CAT activity under oxidative stress. These findings reveal OsUXS3 as a direct target of OsDMI3 and demonstrate its involvement in antioxidant defense.

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