ArticleActa crystallographica. Section F, Structural biology communications2015
Structure of the catalytic domain of Mre11 from Chaetomium thermophilum.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Mechanism of MRX inhibition by Rif2 at telomeres.Nature communications · 2021Article
- Biochemical and structural characterization of analogs of MRE11 breast cancer-associated mutant F237C.Scientific reports · 2021Article
- Pseudomonas putida MPE, a manganese-dependent endonuclease of the binuclear metallophosphoesterase superfamily, incises single-strand DNA in two orientations to yield a mixture of 3'-PO4 and 3'-OH termini.Nucleic acids research · 2021Article
- OsMre11 Is Required for Mitosis during Rice Growth and Development.International journal of molecular sciences · 2020Article
- Article
- Review
- Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.Journal of molecular biology · 2020Article
- Modeling cancer genomic data in yeast reveals selection against ATM function during tumorigenesis.PLoS genetics · 2020Article
- Article
- Activity and structure ofThe Journal of biological chemistry · 2019Article
- The bacterial Mre11-Rad50 homolog SbcCD cleaves opposing strands of DNA by two chemically distinct nuclease reactions.Nucleic acids research · 2018Article
- The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of Damage Signaling and Outcomes to Stress in DNA Replication and Repair.Annual review of biochemistry · 2018Review
- Structurally distinct Mre11 domains mediate MRX functions in resection, end-tethering and DNA damage resistance.Nucleic acids research · 2018Article
- A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex.Protein science : a publication of the Protein Society · 2016Article
- Structural mechanism of ATP-dependent DNA binding and DNA end bridging by eukaryotic Rad50.The EMBO journal · 2016Article
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3 authors.
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Abstract
Together with the Rad50 ATPase, the Mre11 nuclease forms an evolutionarily conserved protein complex that plays a central role in the repair of DNA double-strand breaks (DSBs). Mre11-Rad50 detects and processes DNA ends, and has functions in the tethering as well as the signalling of DSBs. The Mre11 dimer can bind one or two DNA ends or hairpins, and processes DNA endonucleolytically as well as exonucleolytically in the 3'-to-5' direction. Here, the crystal structure of the Mre11 catalytic domain dimer from Chaetomium thermophilum (CtMre11(CD)) is reported. CtMre11(CD) crystals diffracted to 2.8 Å resolution and revealed previously undefined features within the dimer interface, in particular fully ordered eukaryote-specific insertion loops that considerably expand the dimer interface. Furthermore, comparison with other eukaryotic Mre11 structures reveals differences in the conformations of the dimer and the capping domain. In summary, the results reported here provide new insights into the architecture of the eukaryotic Mre11 dimer.
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