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SUMOylation stabilizes the transcription factor DREB2A to improve plant thermotolerance.

  • Wang, Feige1
  • Liu, Yiyang1
  • Shi, Yaqiao1
  • Han, Danlu1
  • Wu, Yuanyuan1
  • Ye, Weixian1
  • Yang, Huanling1
  • Li, Guowei2
  • Cui, Feng3
  • Wan, Shubo3
  • Lai, Jianbin1
  • Yang, Chengwei4
  • 1 South China Normal University CITY: Guangzhou STATE: Guangdong China [CN]. , (China)
  • 2 CNRS/INRA/SupAgro//UM UMR 5004 CITY: Montpellier France [FR]. , (France)
  • 3 Biotechnology Research Center, Shandong Academy of Agricultural Sciences; Shandong Provincial Key Laboratory of Crop Genetic Improvement, Ecology and Physiology CITY: Jinan China [CN]. , (China)
  • 4 South China Normal University CITY: Guangzhou STATE: Guangdong POSTAL_CODE: 510631 China [CN] [email protected] , (China)
Published Article
Plant physiology
Publication Date
Mar 23, 2020
DOI: 10.1104/pp.20.00080
PMID: 32205452


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 PROTEIN 2A (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 is stabilized under high temperature by the post-translational modification SUMOylation. Biochemical data indicated that DREB2A is SUMOylated at K163, a conserved residue adjacent to the negative regulatory domain (NRD) 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. {copyright, serif} 2020 American Society of Plant Biologists. All rights reserved.

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