ArticleThe Journal of biological chemistry2011
Biochemical characterization of bacteriophage T4 Mre11-Rad50 complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- The PhageExpressionAtlas reveals shared and unique transcriptional patterns across phage-host interactions.NAR genomics and bioinformatics · 2026Article
- Basic-patch mutations in bacteriophage T4 Rad50 uncouple ATPase activation from processive nuclease activity.Bioscience reports · 2026Article
- The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.EcoSal Plus · 2025Review
- Dynamic conformations of the P. furiosus MR-DNA complex link Mre11 nuclease activity to DNA-stimulated Rad50 ATP hydrolysis.Communications biology · 2025Article
- Three segment ligation of a 104 kDa multi-domain protein by SrtA and OaAEP1.Journal of biomolecular NMR · 2023Article
- Relations between Structure and Zn(II) Binding Affinity Shed Light on the Mechanisms of Rad50 Hook Domain Functioning and Its Phosphorylation.International journal of molecular sciences · 2022Article
- 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
- Review
- DNA-dependent protein kinase promotes DNA end processing by MRN and CtIP.Science advances · 2020Article
- Processing of DNA Double-Strand Breaks by the MRX Complex in a Chromatin Context.Frontiers in molecular biosciences · 2019Review
- The bacterial Mre11-Rad50 homolog SbcCD cleaves opposing strands of DNA by two chemically distinct nuclease reactions.Nucleic acids research · 2018Article
- 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
- Yeast XRS2 and human NBN gene: Experimental evidence for homology using codon optimized cDNA.PloS one · 2018Article
- Rad50 ATPase activity is regulated by DNA ends and requires coordination of both active sites.Nucleic acids research · 2017Article
- Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly.Scientific reports · 2016Article
- A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex.Protein science : a publication of the Protein Society · 2016Article
- Functional Analysis of the Bacteriophage T4 Rad50 Homolog (gp46) Coiled-coil Domain.The Journal of biological chemistry · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Mre11-Rad50 complex (MR) from bacteriophage T4 (gp46/47) is involved in the processing of DNA double-strand breaks. Here, we describe the activities of the T4 MR complex and its modulation by proteins involved in homologous recombination. T4 Mre11 is a Rad50- and Mn(2+)-dependent dsDNA exonuclease and ssDNA endonuclease. ATP hydrolysis is required for the removal of multiple nucleotides via dsDNA exonuclease activity but not for the removal of the first nucleotide or for ssDNA endonuclease activity, indicating ATP hydrolysis is only required for repetitive nucleotide removal. By itself, Rad50 is a relatively inefficient ATPase, but the presence of Mre11 and dsDNA increases ATP hydrolysis by 20-fold. The ATP hydrolysis reaction exhibits positive cooperativity with Hill coefficients ranging from 1.4 for Rad50 alone to 2.4 for the Rad50-Mre11-DNA complex. Kinetic assays suggest that approximately four nucleotides are removed per ATP hydrolyzed. Directionality assays indicate that the prevailing activity is a 3' to 5' dsDNA exonuclease, which is incompatible with the proposed role of MR in the production of 3' ssDNA ends. Interestingly, we found that in the presence of a recombination mediator protein (UvsY) and ssDNA-binding protein (gp32), Mre11 is capable of using Mg(2+) as a cofactor for its nuclease activity. Additionally, the Mg(2+)-dependent nuclease activity, activated by UvsY and gp32, results in the formation of endonuclease reaction products. These results suggest that gp32 and UvsY may alter divalent cation preference and facilitate the formation of a 3' ssDNA overhang, which is a necessary intermediate for recombination-mediated double-strand break repair.
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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.