SMYD5 catalyzes histone H3 lysine 36 trimethylation at promoters

Yanjun Zhang, Yuan Fang, Yin Tang, Shixun Han, Junqi Jia, Xinyi Wan, Jiaqi Chen, Ying Yuan, Bin Zhao and Dong Fang ()
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Yanjun Zhang: Zhejiang University
Yuan Fang: Zhejiang University
Yin Tang: Zhejiang University
Shixun Han: Zhejiang University
Junqi Jia: Zhejiang University
Xinyi Wan: Zhejiang University
Jiaqi Chen: Zhejiang University School of Medicine
Ying Yuan: Zhejiang University School of Medicine
Bin Zhao: Zhejiang University
Dong Fang: Zhejiang University

Nature Communications, 2022, vol. 13, issue 1, 1-19

Abstract: Abstract Histone marks, carriers of epigenetic information, regulate gene expression. In mammalian cells, H3K36me3 is mainly catalyzed by SETD2 at gene body regions. Here, we find that in addition to gene body regions, H3K36me3 is enriched at promoters in primary cells. Through screening, we identify SMYD5, which is recruited to chromatin by RNA polymerase II, as a methyltransferase catalyzing H3K36me3 at promoters. The enzymatic activity of SMYD5 is dependent on its C-terminal glutamic acid-rich domain. Overexpression of full-length Smyd5, but not the C-terminal domain-truncated Smyd5, restores H3K36me3 at promoters in Smyd5 knockout cells. Furthermore, elevated Smyd5 expression contributes to tumorigenesis in liver hepatocellular carcinoma. Together, our findings identify SMYD5 as the H3K36me3 methyltransferase at promoters that regulates gene expression, providing insights into the localization and function of H3K36me3.

Date: 2022
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DOI: 10.1038/s41467-022-30940-1

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