ArticleGenes & development2023
Structure and DNA-bridging activity of the essential Rec114-Mei4 trimer interface.
Article in Genes & development, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Controlling Meiotic Double-Strand Break Formation in Mice: A Web of Multivalent Protein-Protein Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Mug20-Rec25-Rec27 binds DNA and enhances meiotic DNA break formation via phase-separated condensates.Nucleic acids research · 2025Article
- Cryo-EM structures of the Spo11 core complex bound to DNA.Nature structural & molecular biology · 2025Article
- The TOPOVIBL meiotic DSB formation protein: new insights from its biochemical and structural characterization.Nucleic acids research · 2024Article
- Seeding the meiotic DNA break machinery and initiating recombination on chromosome axes.Nature communications · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
- Essential roles of the ANKRD31-REC114 interaction in meiotic recombination and mouse spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cryo-EM structure of the Spo11 core complex bound to DNA.bioRxiv : the preprint server for biology · 2023Article
- Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes.Genes & development · 2023Article
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7 authors at 3 institutions in 1 country.
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Abstract
The DNA double-strand breaks (DSBs) that initiate meiotic recombination are formed by an evolutionarily conserved suite of factors that includes Rec114 and Mei4 (RM), which regulate DSB formation both spatially and temporally. In vivo, these proteins form large immunostaining foci that are integrated with higher-order chromosome structures. In vitro, they form a 2:1 heterotrimeric complex that binds cooperatively to DNA to form large, dynamic condensates. However, understanding of the atomic structures and dynamic DNA binding properties of RM complexes is lacking. Here, we report a structural model of a heterotrimeric complex of the C terminus of Rec114 with the N terminus of Mei4, supported by nuclear magnetic resonance experiments. This minimal complex, which lacks the predicted intrinsically disordered region of Rec114, is sufficient to bind DNA and form condensates. Single-molecule experiments reveal that the minimal complex can bridge two or more DNA duplexes and can generate force to condense DNA through long-range interactions. AlphaFold2 predicts similar structural models for RM orthologs across diverse taxa despite their low degree of sequence similarity. These findings provide insight into the conserved networks of protein-protein and protein-DNA interactions that enable condensate formation and promote formation of meiotic DSBs.
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