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SANT proteins modulate gene expression by coordinating histone H3KAc and Khib levels and regulate plant heat tolerance

文献类型： 外文期刊

作者： Zhou, Xishi;Fan, Yujin;Zhu, Xiying;Zhao, Ruihua;He, Junna;Li, Pengfeng;Shang, Shengping;Goodrich, Justin;Zhu, Jian-Kang;Zhang, Cui-Jun

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关键词： (1-1-1)

期刊名称： PLANT PHYSIOLOGY

ISSN： 0032-0889

年卷期： 2024 年

页码：

收录情况： SCIE（2024版）

摘要： Histone post-translational modifications (PTMs), such as acetylation and recently identified lysine 2-hydroxyisobutyrylation (Khib), act as active epigenomic marks in plants. SANT domain-containing proteins SANT1, SANT2, SANT3, and SANT4 (SANT1/2/3/4), derived from PIF/Harbinger transposases, form a complex with HISTONE DEACETYLASE 6 (HDA6) to regulate gene expression via histone deacetylation. However, whether SANT1/2/3/4 coordinates different types of PTMs to regulate transcription and mediate responses to specific stresses in plants remains unclear. Here, in addition to modulating histone deacetylation, we found that SANT1/2/3/4 proteins acted like HDA6 or HDA9 in regulating the removal of histone Khib in Arabidopsis (Arabidopsis thaliana). Histone H3 lysine acetylation (H3KAc) and histone Khib were coordinated by SANT1/2/3/4 to regulate gene expression, with H3KAc playing a predominant role and Khib acting complementarily to H3KAc. SANT1/2/3/4 mutation significantly increased the expression of heat-inducible genes with concurrent change of H3KAc levels under normal and heat stress conditions, resulting in enhanced thermotolerance. This study revealed the critical roles of Harbinger transposon-derived SANT domain-containing proteins in transcriptional regulation by coordinating different types of histone PTMs and in the regulation of plant thermotolerance by mediating histone acetylation modification. Proteins containing a histone-tail-binding module coordinate histone lysine acetylation and 2-hydroxyisobutyrylation and play critical roles in transcriptional regulation and plant thermotolerance.

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