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Showing 1–7 of 7 results
Advanced filters: Author: Ulrich Rass Clear advanced filters

  • DNA2 suppresses recombination-restarted replication and checkpoint activation at stalled forks, and its loss triggers recombination-dependent synthesis, checkpoint signalling and cell-cycle exit, highlighting its essential role in proliferation and growth failure in primordial dwarfism.

    • Jessica J. R. Hudson
    • Rowin Appanah
    • Ulrich Rass
    ResearchOpen Access
    Nature
    P: 1-9

  • DNA replication stress drives genome instability and cancer. Here, Ölmezer and colleagues show that the helicase activity of multifunctional enzyme Dna2 suppresses dead-end replication structures that impair chromosome segregation if not removed by Holliday junction resolvase Yen1 in yeast.

    • Gizem Ölmezer
    • Maryna Levikova
    • Ulrich Rass
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-13

  • Structure determination and functional analyses of budding yeast Rif1 reveal a novel, hooked N-terminal DNA-binding domain required for telomere maintenance and checkpoint control and show that Rif1's role in DNA-repair pathway choice is conserved in yeast and mammalian cells.

    • Stefano Mattarocci
    • Julia K Reinert
    • Ulrich Rass
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 588-595

  • Rif1 is involved in different processes such as telomere homeostasis, DNA replication timing, and DNA double strand break (DSB) repair pathway choice. Here, the authors reveal that Rif1 S-acylation facilitates the accumulation of Rif1 at DSBs, attenuation of DNA end-resection, and DSB repair by non-homologous end-joining.

    • Gabriele A. Fontana
    • Daniel Hess
    • Ulrich Rass
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • A four-stranded DNA intermediate, known as a Holliday junction, is formed during meiosis and DNA repair. This structure covalently links two DNA molecules. The product of the RuvC gene in Escherichia coli was shown to be the bacterial Holliday junction resolvase. The mammalian enzyme has remained refractory to identification until now, where GEN1 is identified as the human resolvase.

    • Stephen C. Y. Ip
    • Ulrich Rass
    • Stephen C. West
    Research
    Nature
    Volume: 456, P: 357-361

  • Aprataxin cleans up unfinished DNA ligation intermediates. By cleaving off an adenylate group at the site of a ligatable nick, aprataxin generates ends that can then be re-ligated. This suggests that neurodegeneration results from the accumulation of these intermediates in post-mitotic neuronal cells.

    • Ivan Ahel
    • Ulrich Rass
    • Stephen C. West
    Research
    Nature
    Volume: 443, P: 713-716

  • Holliday junction resolvases lock dynamic DNA four-way junctions into specific structural conformations for symmetric DNA cleavage. Single-molecule studies now reveal that resolvases can relax their grip, enabling Holliday junction conformer transitions and branch migration in the enzyme-bound form.

    • Ulrich Rass
    News & Views
    Nature Chemical Biology
    Volume: 15, P: 209-210