5ZNR

Crystal structure of PtSHL in complex with an H3K27me3 peptide

Summary for 5ZNR

• Entry DOI: 10.2210/pdb5znr/pdb
• Descriptor: SHORT LIFE family protein, 17-mer peptide from Histone H3.2, ZINC ION, ... (4 entities in total)
• Functional Keywords: bah, phd, shl, plant, h3k27me3, epigenetics, gene regulation
• Biological source: Populus trichocarpa (Western balsam poplar); More
• Total number of polymer chains: 4
• Total formula weight: 54252.26

Authors

Lv, X.,Du, J. (deposition date: 2018-04-10, release date: 2018-07-18, Last modification date: 2023-11-22)

Primary citation

Qian, S.,Lv, X.,Scheid, R.N.,Lu, L.,Yang, Z.,Chen, W.,Liu, R.,Boersma, M.D.,Denu, J.M.,Zhong, X.,Du, J.
Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL.
Nat Commun, 9:2425-2425, 2018

PubMed 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.

PubMed: 29930355
DOI: 10.1038/s41467-018-04836-y

Experimental method

X-RAY DIFFRACTION (3.202 Å)