Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles

Weibin Wang, James M. Daley, Youngho Kwon, Danielle S. Krasner, Patrick Sung

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

The budding yeast Mre11-Rad50-Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence onATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX-Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX-Sae2 creates entry sites for the long-range resection machinery.

Original languageEnglish (US)
Pages (from-to)2331-2336
Number of pages6
JournalGenes and Development
Volume31
Issue number23-24
DOIs
StatePublished - Dec 1 2017

Keywords

  • DNA end resection
  • Ku70-Ku80
  • MRX-Sae2
  • Nuclease
  • Nucleosome
  • RPA

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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