ArticleScientific reports2018
A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Basic-patch mutations in bacteriophage T4 Rad50 uncouple ATPase activation from processive nuclease activity.Bioscience reports · 2026Article
- Saccharomyces cerevisiae Xrs2 Binds DNA Through Its FHA Domain.Journal of molecular biology · 2025Article
- Leveraging AlphaFold2 and residual dipolar couplings for side-chain methyl group assignment: A case study with S. cerevisiae Xrs2.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Dynamic conformations of the P. furiosus MR-DNA complex link Mre11 nuclease activity to DNA-stimulated Rad50 ATP hydrolysis.Communications biology · 2025Article
- Review
- Dynamic Properties of the DNA Damage Response Mre11/Rad50 Complex.International journal of molecular sciences · 2023Review
- Three segment ligation of a 104 kDa multi-domain protein by SrtA and OaAEP1.Journal of biomolecular NMR · 2023Article
- Analysis of coordinated NMR chemical shifts to map allosteric regulatory networks in proteins.Methods (San Diego, Calif.) · 2023Article
- Article
- The dynamic nature of the Mre11-Rad50 DNA break repair complex.Progress in biophysics and molecular biology · 2021Review
- Biochemical and structural characterization of analogs of MRE11 breast cancer-associated mutant F237C.Scientific reports · 2021Article
- Article
- Review
- Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.Journal of molecular biology · 2020Article
- The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases.Nucleic acids research · 2020Article
- Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms.Nucleic acids research · 2020Article
- Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020Review
- Functional and structural insights into the MRX/MRN complex, a key player in recognition and repair of DNA double-strand breaks.Computational and structural biotechnology journal · 2020Review
- DNA methylomes and transcriptomes analysis reveal implication of host DNA methylation machinery in BmNPV proliferation in Bombyx mori.BMC genomics · 2019Article
- The ATP-bound conformation of the Mre11-Rad50 complex is essential for Tel1/ATM activation.Nucleic acids research · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Mre11-Rad50 protein complex is an initial responder to sites of DNA double strand breaks. Many studies have shown that ATP binding to Rad50 causes global changes to the Mre11-Rad50 structure, which are important for DNA repair functions. Here we used methyl-based NMR spectroscopy on a series of mutants to describe a dynamic allosteric pathway within Rad50. Mutations result in changes in the side chain methyl group chemical environment that are correlated with altered nanosecond timescale dynamics. We also observe striking relationships between the magnitude of chemical shift perturbations and Rad50 and Mre11 activities. Together, these data suggest an equilibrium between a ground state and an "active" dimerization competent state of Rad50 that has locally altered structure and dynamics and is poised for ATP-induced dimerization and eventual ATP hydrolysis. Thus, this sparsely populated intermediate is critical for Mre11-Rad50-directed DNA double strand break repair.
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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.