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


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.

SUBMITTER: Qian S 

PROVIDER: S-EPMC6013494 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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

Qian Shuiming S   Lv Xinchen X   Scheid Ray N RN   Lu Li L   Yang Zhenlin Z   Chen Wei W   Liu Rui R   Boersma Melissa D MD   Denu John M JM   Zhong Xuehua X   Du Jiamu J  

Nature communications 20180621 1


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  ...[more]

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