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Showing 1–13 of 13 results
Advanced filters: Author: "Patrick Sung" Clear advanced filters
  • The tumour suppressor complex BRCA1–BARD1, which facilitates the generation of a single-stranded DNA template during homologous recombination, also binds to the recombinase RAD51 and enhances its function.

    • Weixing Zhao
    • Justin B. Steinfeld
    • Patrick Sung
    Research
    Nature
    Volume: 550, P: 360-365
  • Tumor suppressor PALB2 is known to interact with BRCA1 and BRCA2, and to be required for the latter's localization to sites of DNA damage. Now PALB2 is shown to bind directly to DNA, to recombinase RAD51 and its accessory factor RAD51AP1. PALB2 also stimulates D loop formation by RAD51 in a synergistic manner with RAD51AP1.

    • Eloïse Dray
    • Julia Etchin
    • Patrick Sung
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1255-1259
  • When double-strand breaks occur in DNA, the broken ends must undergo processing to prepare them for repair. Here, and in an accompanying study, this processing reaction has now been replicated in vitro using yeast proteins. Processing minimally requires the activities of a helicase, a nuclease and a single-strand-binding protein, although the reaction is enhanced by the addition of three factors that help to target the core complex and stimulate the unwinding activity.

    • Hengyao Niu
    • Woo-Hyun Chung
    • Patrick Sung
    Research
    Nature
    Volume: 467, P: 108-111
  • FAN1 is a structure-specific nuclease that plays a major role in eliminating highly cytotoxic interstrand DNA crosslinks. Here, Zhao et al. present several crystal structures of FAN1 in complex with DNA substrates and biochemical analyses that establish how FAN1 functions to resolve interstrand DNA crosslinks.

    • Qi Zhao
    • Xiaoyu Xue
    • Yong Xiong
    Research
    Nature Communications
    Volume: 5, P: 1-9
  • Homologous repair of DNA double strand breaks in Saccharomyces cerevisiaeis dependent on several conserved Rad51 paralogs. Here the authors provide biochemical evidence that Rad55-Rad57 synergistically interacts with the Shu complex to promote Rad51 filament formation and homology directed repair.

    • William A. Gaines
    • Stephen K. Godin
    • Kara A. Bernstein
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-7
  • Resection of DNA 5′ ends is the initial step for repair of double-strand breaks via homologous recombination. DNA resection is controlled in a cell-cycle dependent manner, with yeast Cdk1 known to control Sae2, a nuclease that initiates resection. Now recruitment to DNA damage sites of Dna2, a nuclease responsible for extensive resection, is also shown to be controlled by Cdk1.

    • Xuefeng Chen
    • Hengyao Niu
    • Grzegorz Ira
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1015-1019
  • The conserved MHF1/MHF2 DNA-processing complex is essential for DNA repair in response to genotoxic stress. Here, Zhao et al.report the crystal structure of a human MHF–DNA complex that provides insight into how MHF recognizes branched DNA—a feature important for cellular resistance to DNA damage.

    • Qi Zhao
    • Dorina Saro
    • Yong Xiong
    Research
    Nature Communications
    Volume: 5, P: 1-12
  • Homologous recombination has an important role in DNA repair, DNA replication, meiotic chromosome segregation and telomere maintenance. Its tight regulation by DNA helicases and mediator proteins is essential to avoid cell-cycle arrest, genome destabilization and cancer formation.

    • Patrick Sung
    • Hannah Klein
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 7, P: 739-750
  • The tumor suppressor protein BRCA2 promotes efficient repair of damaged chromosomes by homologous recombination, and it does so by influencing the activity of the Rad51 recombinase. A new biochemical study on the Ustilago maydis BRCA2 ortholog Brh2 sheds light on the molecular function of this tumor suppressor in the Rad51-mediated homologous recombination reaction.

    • Patrick Sung
    News & Views
    Nature Structural & Molecular Biology
    Volume: 12, P: 213-214