ArticleGenes & development2023
Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 24 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
- Insights into the recruitment of the H3K4me3 reader Spp1 by the meiotic double-strand break protein Mer2.Nucleic acids research · 2026Article
- Recruitment of Mre11 to recombination sites during meiosis.Nature communications · 2026Article
- Article
- Mei4 deficiency induces sexual dimorphism in early meiosis and promotes production of unreduced eggs in zebrafish.Zoological research · 2026Article
- Dimerization of thebioRxiv : the preprint server for biology · 2026Article
- Genetic and physical interactions reveal overlapping and distinct contributions to meiotic double-strand break formation inbioRxiv : the preprint server for biology · 2025Article
- Cryo-EM structures of the Spo11 core complex bound to DNA.Nature structural & molecular biology · 2025Article
- Challenges in bridging the gap between protein structure prediction and functional interpretation.Proteins · 2025Article
- The plant early recombinosome: a high security complex to break DNA during meiosis.Plant reproduction · 2024Review
- 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
- Cryo-EM structure of the Spo11 core complex bound to DNA.bioRxiv : the preprint server for biology · 2023Article
- Structure and DNA-bridging activity of the essential Rec114-Mei4 trimer interface.Genes & development · 2023Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Meiosis-specific Rec114-Mei4 and Mer2 complexes are thought to enable Spo11-mediated DNA double-strand break (DSB) formation through a mechanism that involves DNA-dependent condensation. However, the structure, molecular properties, and evolutionary conservation of Rec114-Mei4 and Mer2 are unclear. Here, we present AlphaFold models of Rec114-Mei4 and Mer2 complexes supported by nuclear magnetic resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS), and mutagenesis. We show that dimers composed of the Rec114 C terminus form α-helical chains that cup an N-terminal Mei4 α helix, and that Mer2 forms a parallel homotetrameric coiled coil. Both Rec114-Mei4 and Mer2 bind preferentially to branched DNA substrates, indicative of multivalent protein-DNA interactions. Indeed, the Rec114-Mei4 interaction domain contains two DNA-binding sites that point in opposite directions and drive condensation. The Mer2 coiled-coil domain bridges coaligned DNA duplexes, likely through extensive electrostatic interactions along the length of the coiled coil. Finally, we show that the structures of Rec114-Mei4 and Mer2 are conserved across eukaryotes, while DNA-binding properties vary significantly. This work provides insights into the mechanism whereby Rec114-Mei4 and Mer2 complexes promote the assembly of the meiotic DSB machinery and suggests a model in which Mer2 condensation is the essential driver of assembly, with the DNA-binding activity of Rec114-Mei4 playing a supportive role.
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