J Integr Plant Biol. ›› 2023, Vol. 65 ›› Issue (1): 45-63.DOI: 10.1111/jipb.13372

• Abiotic Stress Responses • Previous Articles     Next Articles

HY5-HDA9 orchestrates the transcription of HsfA2 to modulate salt stress response in Arabidopsis

Jiaheng Yang1†, Xiao Qu1†, Tao Li2†, Yixiang Gao1, Haonan Du1, Lanjie Zheng1, Manchun Ji1, Paifeng Zhang1, Yan Zhang1, Jinxin Hu1, Liangyu Liu3, Zefu Lu4, Zijian Yang3, Huiyong Zhang2, Jianping Yang1*, Yongqing Jiao1*, Xu Zheng1*   

  1. 1. College of Agronomy, State Key Laboratory of Wheat and Maize Crop Science, and Center for Crop Genome Engineering, Longzi Lake Campus Henan Agricultural University Zhengzhou 450046 China;
    2. College of Life Science Henan Agricultural University Zhengzhou 450002 China;
    3. College of Life Sciences Capital Normal University Beijing 100048 China;
    4. Institute of Crop Sciences Chinese Academy of Agricultural Sciences Beijing 100081 China
    These authors contributed equally to this article.
    *Correspondences: Jianping Yang (jpyang@henau.edu.cn); Yongqing Jiao (jiaoyongqing@henau.edu.cn); Xu Zheng (zhengxu@henau.edu.cn, Dr. Zheng is fully responsible for the distribution of the materials associated with this article)
  • Received:2022-08-25 Accepted:2022-09-20 Online:2022-09-27 Published:2023-01-01

Abstract: Integration of light signaling and diverse abiotic stress responses contribute to plant survival in a changing environment. Some reports have indicated that light signals contribute a plant's ability to deal with heat, cold, and stress. However, the molecular link between light signaling and the salt-response pathways remains unclear. We demonstrate here that increasing light intensity elevates the salt stress tolerance of plants. Depletion of HY5, a key component of light signaling, causes Arabidopsis thaliana to become salinity sensitive. Interestingly, the small heat shock protein (sHsp) family genes are upregulated in hy5-215 mutant plants, and HsfA2 is commonly involved in the regulation of these sHsps. We found that HY5 directly binds to the G-box motifs in the HsfA2 promoter, with the cooperation of HISTONE DEACETYLASE 9 (HDA9), to repress its expression. Furthermore, the accumulation of HDA9 and the interaction between HY5 and HDA9 are significantly enhanced by salt stress. On the contrary, high temperature triggers HY5 and HDA9 degradation, which leads to dissociation of HY5-HDA9 from the HsfA2 promoter, thereby reducing salt tolerance. Under salt and heat stress conditions, fine tuning of protein accumulation and an interaction between HY5 and HDA9 regulate HsfA2 expression. This implies that HY5, HDA9, and HsfA2 play important roles in the integration of light signaling with salt stress and heat shock response.

Key words: HDA9, heat shock, HsfA2, HY5, light signaling, salt stress, small Hsps, temperature

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