ArticleThe Journal of biological chemistry2012
ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Basic-patch mutations in bacteriophage T4 Rad50 uncouple ATPase activation from processive nuclease activity.Bioscience reports · 2026Article
- Dynamic conformations of the P. furiosus MR-DNA complex link Mre11 nuclease activity to DNA-stimulated Rad50 ATP hydrolysis.Communications biology · 2025Article
- Critical DNA damaging pathways in tumorigenesis.Seminars in cancer biology · 2022Review
- Structural features of Dnase1L3 responsible for serum antigen clearance.Communications biology · 2022Article
- Take a Break to Repair: A Dip in the World of Double-Strand Break Repair Mechanisms Pointing the Gaze on Archaea.International journal of molecular sciences · 2021Review
- DNA end resection and its role in DNA replication and DSB repair choice in mammalian cells.Experimental & molecular medicine · 2020Review
- Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.Journal of molecular biology · 2020Article
- Stepwise 5' DNA end-specific resection of DNA breaks by the Mre11-Rad50-Xrs2 and Sae2 nuclease ensemble.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Processing of DNA Double-Strand Breaks by the MRX Complex in a Chromatin Context.Frontiers in molecular biosciences · 2019Review
- Purification and Biophysical Characterization of the Mre11-Rad50-Nbs1 Complex.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Physical and functional interplay between PCNA DNA clamp and Mre11-Rad50 complex from the archaeon Pyrococcus furiosus.Nucleic acids research · 2018Article
- A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair.Scientific reports · 2018Article
- Targeting Allostery with Avatars to Design Inhibitors Assessed by Cell Activity: Dissecting MRE11 Endo- and Exonuclease Activities.Methods in enzymology · 2018Article
- A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex.Protein science : a publication of the Protein Society · 2016Article
- Functions and regulation of the MRX complex at DNA double-strand breaks.Microbial cell (Graz, Austria) · 2016Review
- hMSH5 Facilitates the Repair of Camptothecin-induced Double-strand Breaks through an Interaction with FANCJ.The Journal of biological chemistry · 2015Article
- Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repair.Progress in biophysics and molecular biology · 2015Review
- Structure of the Rad50 DNA double-strand break repair protein in complex with DNA.The EMBO journal · 2014Article
- The Mre11/Rad50/Nbs1 complex: recent insights into catalytic activities and ATP-driven conformational changes.Experimental cell research · 2014Review
- Structural studies of DNA end detection and resection in homologous recombination.Cold Spring Harbor perspectives in biology · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
MRE11-RAD50 is a key early response protein for processing DNA ends of broken chromosomes for repair, yet how RAD50 nucleotide dynamics regulate MRE11 nuclease activity is poorly understood. We report here that ATP binding and ATP hydrolysis cause a striking butterfly-like opening and closing of the RAD50 subunits, and each structural state has a dramatic functional effect on MRE11. RAD50-MRE11 has an extended conformation in solution when MRE11 is an active nuclease. However, ATP binding to RAD50 induces a closed conformation, and in this state MRE11 is an endonuclease. ATP hydrolysis opens the RAD50-MRE11 complex, and MRE11 maintains exonuclease activity. Thus, ATP hydrolysis is a molecular switch that converts MRE11 from an endonuclease to an exonuclease. We propose a testable model in which the open-closed transitions are used by RAD50-MRE11 to discriminate among DNA ends and drive the choice of recombination pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.