Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-04836-y
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Funding
- National Key R&D Program of China [2016YFA0503200]
- National Natural Science Foundation of China [31622032, 31770782]
- Chinese Academy of Sciences
- Alexander von Humboldt Foundation
- NSF CAREER award [MCB-1552455]
- NIH Maximizing Investigators' Research Award [R35GM124806]
- NIH [GM059785-15/P250VA]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM059785, R35GM124806, R01GM059785, T32GM007133] Funding Source: NIH RePORTER
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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.
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