SUMOylation Stabilizes the Transcription Factor DREB2A to Improve Plant Thermotolerance

SUMOylation Stabilizes the Transcription Factor DREB2A to Improve Plant Thermotolerance
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SUMOylation 稳定转录因子 DREB2A 以提高植物耐热性

DOI:
10.1104/pp.20.00080
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发表时间:
2020
期刊:
影响因子:
7.4
通讯作者:
Yang Chengwei
Yang Chengwei
中科院分区:
生物学1区
文献类型:
--
作者:
Wang Feige;Liu Yiyang;Shi Yaqiao;Han Danlu;Wu Yuanyuan;Ye Weixian;Yang Huanling;Li Guowei;Cui Feng;Wan Shubo;Lai Jianbin;Yang Chengwei

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高温胁迫严重影响植物的生长发育,造成严重的农业损失。一个关键的转录因子网络参与植物对高温的适应。脱水反应元件结合蛋白2A(DREB 2A)是植物耐热性的关键转录因子。DREB 2A蛋白在常温下不稳定,并被26 S蛋白酶体降解;然而,DREB 2A蛋白稳定性响应HS而显著增加的机制仍然知之甚少。在本研究中,我们发现拟南芥DREB 2A蛋白通过翻译后修饰SUMO化而在高温下保持稳定。生化数据表明DREB 2A在K163处SUMO化,K163是HS期间邻近负调控结构域的保守残基。DREB 2A的SUMO化抑制其与BPM 2(泛素连接酶组分)的相互作用,从而增加DREB 2A蛋白在高温下的稳定性。此外,对植物耐热性和标记基因表达的分析表明DREB 2A SUMO化对其在HS反应中的功能是必需的。总的来说,我们的数据揭示了SUMO化在高温下维持DREB 2A稳定性中的作用,从而提高了我们对植物细胞HS反应的调控机制的理解。
Heat stress (HS) has serious effects on plant development, resulting in heavy agricultural losses. A critical transcription factor network is involved in plant adaptation to high temperature. DEHYDRATION RESPONSIVE ELEMENT-BINDING PROTEIN2A (DREB2A) is a key transcription factor that functions in plant thermotolerance. The DREB2A protein is unstable under normal temperature and is degraded by the 26S proteasome; however, the mechanism by which DREB2A protein stability dramatically increases in response to HS remains poorly understood. In this study, we found that the DREB2A protein of Arabidopsis (Arabidopsis thaliana) is stabilized under high temperature by the posttranslational modification SUMOylation. Biochemical data indicated that DREB2A is SUMOylated at K163, a conserved residue adjacent to the negative regulatory domain during HS. SUMOylation of DREB2A suppresses its interaction with BPM2, a ubiquitin ligase component, consequently increasing DREB2A protein stability under high temperature. In addition, analysis of plant heat tolerance and marker gene expression indicated that DREB2A SUMOylation is essential for its function in the HS response. Collectively, our data reveal a role for SUMOylation in the maintenance of DREB2A stability under high temperature, thus improving our understanding of the regulatory mechanisms underlying HS response in plant cells.