ArticleNature communications2025
Mechanism of Rad51 filament formation by Rad52 and Rad55-Rad57 in homologous recombination.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- R-loops and D-loops: a delicate balance in genomic stability and instability.Cell communication and signaling : CCS · 2026Review
- Direct evidence and quantification of homologous recognition between DNA duplexes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- OT-Curtains: an approach for studying protein interactions with DNA ends using optical tweezers and confocal fluorescence microscopy.Nucleic acids research · 2026Article
- A phosphorylation switch at MRE11 links ATM-ATR and calcium signaling to safeguard stalled replication fork stability.Research square · 2026Article
- Enhancement of single-stranded template annealing activity by Rad52 during repair of CRISPR-induced dsDNA breaks.Nucleic acids research · 2026Article
- Interplay Between Poly(ADP-ribosyl)ation and Specific Inner Cellular Events That Suggest Combination Strategies for Overcoming PARP Inhibitor Resistance.Pharmaceutics · 2026Review
- Particulate Hexavalent Chromium Inhibits RAD51 Paralogs Necessary for RAD51 Filament Formation and Stabilization During Homologous Recombination Repair.Occupational Health · 2026Article
- The human RAD52 complex undergoes phase separation and facilitates bundling and end-to-end tethering of RAD51 presynaptic filaments.Nucleic acids research · 2026Article
- Double jeopardy: howFrontiers in cell and developmental biology · 2026Review
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Authors and funding
14 authors.
Funding
Abstract
Homologous recombination (HR) repairs double-stranded DNA breaks (DSBs) by generating single-stranded DNA (ssDNA), which is initially coated by Replication Protein A (Rpa). Rad51, a recombinase, catalyzes strand invasion but binds ssDNA with lower affinity than Rpa, necessitating mediator proteins like Rad52 (yeast) or BRCA2 (humans) for Rad51 loading. The mechanisms of this exchange remain unclear. We show that Saccharomyces cerevisiae Rad52 uses its disordered C-terminus to sort polydisperse Rad51 into discrete monomers. Using fluorescent-Rad51 and single-molecule optical tweezers, we visualize Rad52-mediated Rad51 filament formation on Rpa-coated ssDNA, preferentially at ssDNA-dsDNA junctions. Deleting the C-terminus of Rad52 disrupts Rad51 sorting and loading. Addition of the Rad51 paralog Rad55-Rad57 enhances Rad51 binding by ~60%. Despite structural differences, Rad52 and BRCA2 share conserved functional features. We propose a unified "Sort, Stack & Extend" (SSE) mechanism by which mediator proteins and paralogs coordinate Rad51 filament assembly during HR.
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