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- Title
Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL.
- Authors
Shuiming Qian; Xinchen Lv; Scheid, Ray N.; Li Lu; Zhenlin Yang; Wei Chen; Rui Liu; Boersma, Melissa D.; Denu, John M.; Xuehua Zhong; Jiamu Du
- 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.
- Subjects
HISTONES; CHROMATIN; GENE expression; POST-translational modification; HOMOLOGY (Biology)
- Publication
Nature Communications, 2018, Vol 9, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-018-04836-y