9MYP

Structure of Patiria miniata Hop1 chromatin binding region

Summary for 9MYP

• Entry DOI: 10.2210/pdb9myp/pdb
• Descriptor: HORMA domain-containing protein, ZINC ION, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: meiosis, phd domain, winged-helix domain, dna binding protein
• Biological source: Patiria miniata (bat star)
• Total number of polymer chains: 3
• Total formula weight: 58265.40

Authors

Rodriguez, A.R.,Ye, Q.,Nguyen, J.,Chau, K.,Corbett, K.D. (deposition date: 2025-01-22, release date: 2025-08-13, Last modification date: 2025-10-15)

Primary citation

Rodriguez, A.A.,Cirulli, A.E.,Chau, K.,Nguyen, J.,Ye, Q.,Corbett, K.D.
Bipartite chromatin recognition by Hop1 from two diverged Holozoa.
Life Sci Alliance, 8:-, 2025

PubMed Abstract: In meiosis, ploidy reduction is driven by a complex series of DNA breakage and recombination events between homologous chromosomes, orchestrated by meiotic HORMA domain proteins (HORMADs). Meiotic HORMADs possess a central chromatin binding region (CBR) whose architecture varies across eukaryotic groups. Here, we determine high-resolution crystal structures of the meiotic HORMAD CBR from two diverged aquatic Holozoa, and , which reveal tightly associated plant homeodomain (PHD) and winged helix-turn-helix (wHTH) domains. We show that PHD-wHTH CBRs bind duplex DNA through their wHTH domains, and identify key residues that disrupt this interaction. Combining experimental and predicted structures, we show that the CBRs' PHDs likely interact with the tail of histone H3, and may discriminate between unmethylated and trimethylated H3 lysine 4. Finally, we show that Holozoa Hop1 CBRs bind nucleosomes in vitro in a bipartite manner involving both the PHD and wHTH domain. Our data reveal how meiotic HORMADs with PHD-wHTH CBRs can bind chromatin and potentially discriminate between chromatin states to drive meiotic recombination to specific chromosomal regions.

PubMed: 40829932
DOI: 10.26508/lsa.202503428

Experimental method

X-RAY DIFFRACTION (1.84 Å)