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Genes Dev. 2017 Dec 1;31(23-24):2331-2336. doi: 10.1101/gad.307900.117. Epub 2018 Jan 10.

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

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.

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 on ATP 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.

KEYWORDS:

DNA end resection; Ku70–Ku80; MRX–Sae2; RPA; nuclease; nucleosome

PMID:
29321177
PMCID:
PMC5795780
DOI:
10.1101/gad.307900.117
[Indexed for MEDLINE]
Free PMC Article

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