Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL

Shuiming Qian, Xinchen Lv, Ray N. Scheid, Li Lu, Zhenlin Yang, Wei Chen, Rui Liu, Melissa D. Boersma, John M. Denu, Xuehua Zhong () and Jiamu Du ()
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Shuiming Qian: University of Wisconsin-Madison
Xinchen Lv: Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Ray N. Scheid: University of Wisconsin-Madison
Li Lu: University of Wisconsin-Madison
Zhenlin Yang: Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Wei Chen: Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Rui Liu: Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Melissa D. Boersma: University of Wisconsin-Madison
John M. Denu: University of Wisconsin-Madison
Xuehua Zhong: University of Wisconsin-Madison
Jiamu Du: Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract The ability of a cell to dynamically switch its chromatin between different functional states constitutes a key mechanism regulating gene expression. Histone mark “readers” display distinct binding specificity to different histone modifications and play critical roles in regulating chromatin states. Here, we show a plant-specific histone reader SHORT LIFE (SHL) capable of recognizing both H3K27me3 and H3K4me3 via its bromo-adjacent homology (BAH) and plant homeodomain (PHD) domains, respectively. Detailed biochemical and structural studies suggest a binding mechanism that is mutually exclusive for either H3K4me3 or H3K27me3. Furthermore, we show a genome-wide co-localization of SHL with H3K27me3 and H3K4me3, and that BAH-H3K27me3 and PHD-H3K4me3 interactions are important for SHL-mediated floral repression. Together, our study establishes BAH-PHD cassette as a dual histone methyl-lysine binding module that is distinct from others in recognizing both active and repressive histone marks.

Date: 2018
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DOI: 10.1038/s41467-018-04836-y

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