AmCBF1 activates the expression of GhClpR1 to mediate dark-green leaves in cotton (Gossypium hirsutum)

文献类型： 外文期刊

第一作者： Zhang, Qianqian

作者： Zhang, Qianqian;Wang, Peilin;Li, Weilong;Liu, Man;Zhou, Lili;Su, Xiaofeng;Cheng, Hongmei;Guo, Huiming;Zhang, Qianqian;Liu, Man;Wang, Peilin;Cheng, Hongmei;Guo, Huiming;Zhou, Lili

作者机构：

关键词： Cotton; Chloroplast; GhClpR1; AmCBF1; Transcription factor

期刊名称：PLANT CELL REPORTS （ 影响因子：6.2； 五年影响因子：5.9 ）

ISSN： 0721-7714

年卷期： 2024 年 43 卷 3 期

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收录情况： SCI

摘要： The ATP-dependent caseinolytic protease (Clp protease) family plays a crucial role within chloroplasts, comprising several Clp proteins to maintain chloroplast homeostasis. At present, research on Clp proteins mainly focuses on Arabidopsis, leaving its function in other plants, particularly in crops, less explored. In this study, we overexpressed AmCBF1 from Ammopiptanthus mongolicus (A. mongolicus) in wild type (R15), and found a significant darkening of leaf colour in transgenic plants (L28 and L30). RNA-seq analysis showed an enrichment of pathways associated with photosynthesis. Subsequent screening of differentially expressed genes revealed a significant up-regulation of GhClpR1, a gene linked to chloroplast development, in the transgenic strain. In addition, GhClpR1 was consistently expressed in upland cotton, with the highest expression observed in leaves. Subcellular localization analysis revealed that the protein encoded by GhClpR1 was located in chloroplasts. Yeast one hybrid and dual luciferase experiments showed that the AmCBF1 transcription factor positively regulates the expression of GhClpR1. VIGs-mediated silencing of GhClpR1 led to a significant yellowing phenotype in the leaves. This was accompanied by a reduction in chlorophyll content, and microscopic examination of chloroplast ultrastructure revealed severe developmental impairment. Finally, yeast two-hybrid assays showed that GhClpR1 interacts with the Clp protease complex accessory protein GhClpT2. Our study provides a foundation for studying the function of the Clp protease complex and a new strategy for cultivating high-light-efficiency cotton resources.

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