ArticleNature structural & molecular biology2025
Cryo-EM structures of the Spo11 core complex bound to DNA.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- 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
- MRE11 suppresses germline mutagenesis at meiotic double-strand breaks in mice.Genes & development · 2026Article
- Multifaceted and evolutionarily dynamic interactions betweenbioRxiv : the preprint server for biology · 2026Article
- Crossover control: A key to unlocking genetic diversity in plant breeding.Journal of integrative plant biology · 2026Review
- Predicting protein-nucleic acid interactions via protein language models with biophysical and evolutionary priors.iScience · 2026Article
- Supercoiled DNA recognition and cleavage control in topoisomerase VI.Nature communications · 2026Article
- MRE11 suppresses germline mutagenesis at meiotic double-strand breaks in mice.bioRxiv : the preprint server for biology · 2026Article
- Dimerization of thebioRxiv : the preprint server for biology · 2026Article
- Structure-informed evolutionary analysis of the meiotic recombination machinery.bioRxiv : the preprint server for biology · 2025Article
- Mouse MRE11-RAD50-NBS1 is needed to start and extend meiotic DNA end resection.Nature communications · 2025Article
- Spo11: from topoisomerase VI to meiotic recombination initiator.Biochemical Society transactions · 2025Review
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- Reconstitution of SPO11-dependent double-strand break formation.bioRxiv : the preprint server for biology · 2024Article
- The TOPOVIBL meiotic DSB formation protein: new insights from its biochemical and structural characterization.Nucleic acids research · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
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9 authors.
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Abstract
DNA double-strand breaks that initiate meiotic recombination are formed by the topoisomerase-relative enzyme Spo11, supported by conserved auxiliary factors. Because high-resolution structural data have not been available, many questions remain about the architecture of Spo11 and its partners and how they engage with DNA. We report cryo-electron microscopy structures at up to 3.3-Å resolution of DNA-bound core complexes of Saccharomyces cerevisiae Spo11 with Rec102, Rec104 and Ski8. In these structures, monomeric core complexes make extensive contacts with the DNA backbone and with the recessed 3'-OH and first 5' overhanging nucleotide, establishing the molecular determinants of DNA end-binding specificity and providing insight into DNA cleavage preferences in vivo. The structures of individual subunits and their interfaces, supported by functional data in yeast, provide insight into the role of metal ions in DNA binding and uncover unexpected structural variation in homologs of the Top6BL component of the core complex.
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