5Z8N

Crystal structure of Arabidopsis thaliana EBS C-terminal deletion construct in complex with an H3K4me2 peptide

Summary for 5Z8N

• Entry DOI: 10.2210/pdb5z8n/pdb
• Descriptor: Chromatin remodeling protein EBS, H3K4me2 peptide, ZINC ION (3 entities in total)
• Functional Keywords: ebs, bah, phd, h3k4me2, histone reader, gene regulation
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 6
• Total formula weight: 73111.27

Authors

Yang, Z.,Du, J. (deposition date: 2018-01-31, release date: 2018-07-25, Last modification date: 2023-11-22)

Primary citation

Yang, Z.,Qian, S.,Scheid, R.N.,Lu, L.,Chen, X.,Liu, R.,Du, X.,Lv, X.,Boersma, M.D.,Scalf, M.,Smith, L.M.,Denu, J.M.,Du, J.,Zhong, X.
EBS is a bivalent histone reader that regulates floral phase transition in Arabidopsis.
Nat. Genet., 50:1247-1253, 2018

PubMed Abstract: The ability of cells to perceive and translate versatile cues into differential chromatin and transcriptional states is critical for many biological processes. In plants, timely transition to a flowering state is crucial for successful reproduction. EARLY BOLTING IN SHORT DAY (EBS) is a negative transcriptional regulator that prevents premature flowering in Arabidopsis thaliana. We found that EBS contains bivalent bromo-adjacent homology (BAH)-plant homeodomain (PHD) reader modules that bind H3K27me3 and H3K4me3, respectively. We observed co-enrichment of a subset of EBS-associated genes with H3K4me3, H3K27me3, and Polycomb repressor complex 2 (PRC2). Notably, EBS adopted an autoinhibition mode to mediate its switch in binding preference between H3K27me3 and H3K4me3. This binding balance was critical because disruption of either EBS-H3K27me3 or EBS-H3K4me3 interaction induced early floral transition. Our results identify a bivalent chromatin reader capable of recognizing two antagonistic histone marks, and we propose a distinct mechanism of interaction between active and repressive chromatin states.

PubMed: 30082787
DOI: 10.1038/s41588-018-0187-8

Experimental method

X-RAY DIFFRACTION (3.1 Å)