Structural highlights
Function
H31_ARATH
Publication Abstract from PubMed
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.
Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL.,Qian S, Lv X, Scheid RN, Lu L, Yang Z, Chen W, Liu R, Boersma MD, Denu JM, Zhong X, Du J Nat Commun. 2018 Jun 21;9(1):2425. doi: 10.1038/s41467-018-04836-y. PMID:29930355[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qian S, Lv X, Scheid RN, Lu L, Yang Z, Chen W, Liu R, Boersma MD, Denu JM, Zhong X, Du J. Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL. Nat Commun. 2018 Jun 21;9(1):2425. doi: 10.1038/s41467-018-04836-y. PMID:29930355 doi:http://dx.doi.org/10.1038/s41467-018-04836-y
