Structural and functional characterization of the Spo11 core complex
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Abstract
Spo11, which makes DNA double-strand breaks (DSBs) that are essential for meiotic recombination, has long been recalcitrant to biochemical study. We provide molecular analysis of Saccharomyces cerevisiae Spo11 purified with partners Rec102, Rec104 and Ski8. Rec102 and Rec104 jointly resemble the B subunit of archaeal topoisomerase VI, with Rec104 occupying a position similar to the Top6B GHKL-type ATPase domain. Unexpectedly, the Spo11 complex is monomeric (1:1:1:1 stoichiometry), consistent with dimerization controlling DSB formation. Reconstitution of DNA binding reveals topoisomerase-like preferences for duplex-duplex junctions and bent DNA. Spo11 also binds noncovalently but with high affinity to DNA ends mimicking cleavage products, suggesting a mechanism to cap DSB ends. Mutations that reduce DNA binding in vitro attenuate DSB formation, alter DSB processing and reshape the DSB landscape in vivo. Our data reveal structural and functional similarities between the Spo11 core complex and Topo VI, but also highlight differences reflecting their distinct biological roles.
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The model of Spo11-Ski8 resembles a previous model based on the Ski3-Ski8 complex, with Ski8 contacting a sequence in Ski3 similar to QREIF380 in Spo11, but suggests a more extensive interaction surface involving an insertion in Ski8 present in Saccharomyces species but not in Schizosaccharomyces pombe and Sordaria macrospora.
“Our model resembles a previous model based on the Ski3–Ski8 complex, with Ski8 contacting a sequence in Ski3 that is similar to the sequence QREIF380 in Spo11 (27,28) (fig. S17A), but suggests a more extensive interaction surface than previously appreciated, involving an insertion in Ski8 that is present in Saccharomyces species but not in Schizosaccharomyces pombe and Sordaria macrospora, where”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [27]
The model clarifies the Spo11 portion of the Rec102-Spo11 interface, which was not well structured in previous homology models.
“The model clarifies the Spo11 portion of this interface, which was not well structured in previous homology models (27,31).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [27]
The predicted Spo11-Ski8 structure is supported by crosslinking and mutagenesis data.
“The predicted Spo11–Ski8 structure is supported by crosslinking and mutagenesis data (26,27).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [27]
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Computed structures of core eukaryotic protein complexes
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- Authors
- Claeys Bouuaert, C., Tischfield, S. E., Pu, S., Mimitou, E. P., Arias-Palomo, E., Berger, J. M., & Keeney, S.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Johns Hopkins University (US)
- Corresponding author
- Keeney, Scott
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2021-01
- Volume
- 28
- Issue
- 1
- Pages
- 92-102
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC7855791
- OpenAlex
- W3120715541
- Cited by
- 87
- References
- 81
- Citations by year
- 2026: 14 · 2025: 15 · 2024: 20 · 2023: 15 · 2022: 9 · 2021: 11 · 2020: 3
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Libraries (submittedVersion, other-oa)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Funders
- Howard Hughes Medical Institute (P30 CA08748)
- Yale University
- Memorial Sloan-Kettering Cancer Center (P30-CA08748)
- National Institutes of Health (2r01ca077373-22, CA08748)
- National Cancer Institute (R01-CA077373, P30-CA-08748, CA08748, CA0777373, P30CA008748)
- National Institute of General Medical Sciences (R35GM118092)
- National Center for Research Resources (S10RR023748)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer therapeutics and mechanisms
- Keywords
- Spo11, DNA double-strand breaks, meiotic recombination, protein complex stoichiometry, protein-DNA interactions, bent DNA, Saccharomyces cerevisiae
- MeSH terms
- Meiotic Recombination Protein SPO11, DNA Topoisomerases, Type II, DNA-Binding Proteins, Endodeoxyribonucleases, Meiosis, Mutation, Nucleic Acid Conformation, Saccharomyces cerevisiae, Microscopy, Atomic Force, Archaeal Proteins, Saccharomyces cerevisiae Proteins, Recombinases, DNA Breaks, Double-Stranded
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