Phosphorylation of 399S at CsHsp70 of Cymbidium sinense is essential to maintain chlorophyll stability

文献类型： 外文期刊

第一作者： Gao, Jie

作者： Gao, Jie;Lu, Chuqiao;Wei, Yonglu;Xie, Qi;Jin, Jianpeng;Li, Jie;Yang, Fengxi;Zhu, Genfa

作者机构：

关键词： Cymbidium sinense; Proteomics; Phosphoproteomics; Leaf variegation; Heat-shock protein 70

期刊名称：PLANT PHYSIOLOGY AND BIOCHEMISTRY （ 影响因子：6.5； 五年影响因子：6.4 ）

ISSN： 0981-9428

年卷期： 2024 年 211 卷

页码：

收录情况： SCI

摘要： The Chinese orchids symbolise nobility and gentility in China, and the variation of leaf color makes Cymbidium sinense more diversified and valuable. However, its color variations especially at the protein level still remain largely unexplored. In this study, the proteomics and phosphoproteomics of Cymbidium sinense leaf color variation mutants were studied. A total of 1059 differentially abundant proteins (DAPs) and 1127 differentially abundant phosphorylation sites belonging to 644 phosphoproteins (DAPPs) were identified in the yellow section of leaf variegation mutant of Cymbidium sinense (MY) compared with the green section (MG). Moreover, 349 coexpressing proteins were found in both omics' datasets, while only 26 proteins showed the same expression patterns in the two omics. The interaction network analysis of kinases and phosphatases showed that DAPs and DAPPs in photosynthesis, response to hormones, pigment metabolic process, phosphorylation, glucose metabolic process, and dephosphorylation might contribute to leaf color variation. The abundance of 28 Hsps and 28 phosphorylation sites belonging to 10 Hsps showed significant differences between MG and MY. CsHsp70 was selected to explore the function in Cymbidium sinense leaf variegation. The results showed CsHsp70 is essential for maintaining photosynthetic pigment content and the 399S phosphorylation site is crucial to the function of CsHsp70. Collectively, our findings construct a comprehensive coverage of protein and protein phosphorylation in leaf variegation of C. sinense, providing valuable insights into its formation mechanisms.

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