ArticleCommunications biology2025
Dynamic conformations of the P. furiosus MR-DNA complex link Mre11 nuclease activity to DNA-stimulated Rad50 ATP hydrolysis.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Basic-patch mutations in bacteriophage T4 Rad50 uncouple ATPase activation from processive nuclease activity.Bioscience reports · 2026Article
- Review
- DNA Modulates Structural Transitions and Oligomerization Kinetics of the Functional Amyloid CRES.Journal of the American Chemical Society · 2026Article
- RAD50 missense variants differentially affect the DNA damage response and mitotic progression.FEBS letters · 2025Article
- Saccharomyces cerevisiae Xrs2 Binds DNA Through Its FHA Domain.Journal of molecular biology · 2025Article
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Authors and funding
5 authors.
Funding
Abstract
The MRE11-RAD50-NBS1/Xrs2 (MRN/X) protein complex has essential roles in the repair of damaged DNA. The current understanding of the conformational landscape of the core MR complex comes from various structural studies. However, given the heterogeneous nature of these structures, we suspect that several conformational states may still be unaccounted for. Here, we use methyl-based NMR experiments on P. furiosus MR to determine an ensemble of distinct conformations of MR bound to DNA, consistent with the highly dynamic nature of the MR-DNA complex. Interrogation of these structures via in vitro activity assays on MR mutants reveal an unexpected, striking correlation between the nuclease activity of Mre11 and the magnitude of DNA-stimulated ATP hydrolysis by Rad50. Together, the structures and activity data support a model for MR activity where DNA-stimulated ATP hydrolysis unlocks Rad50 to provide access to the Mre11 active sites and further demonstrate how a heterogeneous ensemble of conformations can be used to coordinate various functions to direct biological outcomes. By elucidating the dynamic conformations of the DNA-bound MR complex, this work lays the foundation for future studies aimed at further characterizing this landscape and dissecting its role in the molecular mechanism of DNA repair and genome stability.
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Registered trials
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