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<p>Stalled replication forks are processed in post-replication repair by homologous recombination, fork regression, and translesion DNA synthesis. However, the regulation of pathway usage is not fully understood. Rad51 protein maintains genomic stability through its roles in recombination and in protecting stalled replication forks. We report isolation of mutations in <i>Saccharomyces cerevisiae</i> Rad51 that shift post-replication repair from recombination to alternate pathways including mutagenic translesion synthesis. Rad51-E135D and Rad51-K305N show near normal in vitro recombination despite changes in their DNA binding profiles, in particular to dsDNA. The mutants lead to a defect in Rad51 recruitment to stalled forks in vivo as well as a defect in the protection of dsDNA from degradation by Dna2-Sgs1 and Exo1 in vitro. Together, the evidence suggests that Rad51 binding to duplex DNA is critical to control pathway usage at stalled replication forks.</p>

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Rad51 determines pathway usage in post-replication repair

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年1月10日

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  • Damon Meyer,
  • Steven K. Gore,
  • Jie Liu,
  • Shannon J. Ceballos,
  • Shih-Hsun Hung,
  • Giordano Reginato,
  • Maria I. Cano-Linares,
  • Katarzyna H. Maslowska,
  • Florencia Villafañez,
  • Clare Fasching,
  • Christopher Ede,
  • Vincent Pagès,
  • Felix Prado,
  • Petr Cejka,
  • Wolf-Dietrich Heyer

摘要

Stalled replication forks are processed in post-replication repair by homologous recombination, fork regression, and translesion DNA synthesis. However, the regulation of pathway usage is not fully understood. Rad51 protein maintains genomic stability through its roles in recombination and in protecting stalled replication forks. We report isolation of mutations in Saccharomyces cerevisiae Rad51 that shift post-replication repair from recombination to alternate pathways including mutagenic translesion synthesis. Rad51-E135D and Rad51-K305N show near normal in vitro recombination despite changes in their DNA binding profiles, in particular to dsDNA. The mutants lead to a defect in Rad51 recruitment to stalled forks in vivo as well as a defect in the protection of dsDNA from degradation by Dna2-Sgs1 and Exo1 in vitro. Together, the evidence suggests that Rad51 binding to duplex DNA is critical to control pathway usage at stalled replication forks.