Biochemical characterisation of Mer3 helicase interactions and the protection of meiotic recombination intermediates
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Abstract
Crossing over between homologs is critical for the stable segregation of chromosomes during the first meiotic division. Saccharomyces cerevisiae Mer3 (HFM1 in mammals) is a SF2 helicase and member of the ZMM group of proteins, that facilitates the formation of the majority of crossovers during meiosis. Here, we describe the structural organisation of Mer3 and using AlphaFold modelling and XL-MS we further characterise the previously described interaction with Mlh1–Mlh2. We find that Mer3 also forms a previously undescribed complex with the recombination regulating factors Top3 and Rmi1 and that this interaction is competitive with Sgs1BLM helicase. Using in vitro reconstituted D-loop assays we show that Mer3 inhibits the anti-recombination activity of Sgs1 helicase, but only in the presence of Dmc1. Thus we provide a mechanism whereby Mer3 interacts with a network of proteins to protect Dmc1 derived D-loops from dissolution.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Grimm, M., Zimniak, T., Kahraman, A., & Herzog, F. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv463 · Cited by 121 · see citing works
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- Authors
- Altmannova, V., Firlej, M., Müller, F., Janning, P., Rauleder, R., Rousova, D., Schäffler, A., Bange, T., & Weir, J. R.
- Affiliations
- Friedrich Miescher Laboratory of the Max Planck Society , Max-Planck-Ring 9, 72076 Tübingen, Germany
- Max Planck Society (DE)
- Max Planck Institute of Molecular Physiology (DE)
- Institut für Medizinische Psychologie (DE)
- Corresponding author
- Weir, John R
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2023-03-21
- Volume
- 51
- Issue
- 9
- Pages
- 4363-4384
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC10201424
- OpenAlex
- W4328049435
- Cited by
- 15
- References
- 2
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 2 · 2023: 3
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Max Planck Society and the German Research Foundation (WE 6513/2-1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- meiotic recombination, crossing over, Sgs1 helicase, BLM helicase, DMC1, protein-protein interaction, Saccharomyces cerevisiae
- MeSH terms
- MutL Proteins, MutL Protein Homolog 1, Binding, Competitive, Crossing Over, Genetic, DNA Helicases, DNA-Binding Proteins, Meiosis, Protein Binding, Saccharomyces cerevisiae, Protein Folding, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, RecQ Helicases, Homologous Recombination
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