Uncovering the mechanistic basis for specific recognition of monomethylated H3K4 by the CW domain of Arabidopsis histone methyltransferase SDG8

The Journal of Biological Chemistry
Yanchao Liu, Ying Huang

Abstract

Chromatin consists of DNA and histones, and specific histone modifications that determine chromatin structure and activity are regulated by three types of proteins, called writer, reader, and eraser. Histone reader proteins from vertebrates, vertebrate-infecting parasites, and higher plants possess a CW domain, which has been reported to read histone H3 lysine 4 (H3K4). The CW domain of Arabidopsis SDG8 (also called ASHH2), a histone H3 lysine 36 methyltransferase, preferentially binds monomethylated H3K4 (H3K4me1), unlike the mammalian CW domain protein, which binds trimethylated H3K4 (H3K4me3). However, the molecular basis of the selective binding by the CW domain of SDG8 (SDG8-CW) remains unclear. Here, we solved the 1.6-Å-resolution structure of SDG8-CW in complex with H3K4me1, which revealed that residues in the C-terminal α-helix of SDG8-CW determine binding specificity for low methylation levels at H3K4. Moreover, substitutions of key residues, specifically Ile-915 and Asn-916, converted SDG8-CW binding preference from H3K4me1 to H3K4me3. Sequence alignment and mutagenesis studies revealed that the CW domain of SDG725, the homolog of SDG8 in rice, shares the same binding preference with SDG8-CW, indicating that preferenc...Continue Reading

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Citations

May 31, 2020·International Journal of Molecular Sciences·Helena G SilvaM Manuela R Costa
May 26, 2018·The Plant Journal : for Cell and Molecular Biology·Ling JiangChunlin Liu
Jun 17, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xiaofeng FangCaroline Dean
Apr 30, 2021·Journal of Integrative Plant Biology·Yuhua WangJiamu Du
Dec 18, 2021·Frontiers in Plant Science·Huihui FangGang Wu

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