Journal
MOLECULAR CELL
Volume 50, Issue 4, Pages 589-600Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2013.04.032
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Funding
- National Institutes of Health [GM041784]
- European Research Council under the European Union's Seventh Framework Programme (FP7)/ERC [242905]
- European Research Council (ERC) [242905] Funding Source: European Research Council (ERC)
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Replication protein A (RPA) is an essential eukaryotic single-stranded DNA binding protein with a central role in DNA metabolism. RPA directly participates in DNA double-strand break repair by stimulating 5'-3' end resection by the Sgs1/BLM helicase and Dna2 endonuclease in vitro. Here we investigated the role of RPA in end resection in vivo, using a heat-inducible degron system that allows rapid conditional depletion of RPA in Saccharomyces cerevisiae. We found that RPA depletion eliminated both the Sgs1-Dna2-and Exo1-dependent extensive resection pathways and synergized with mre11 Delta to prevent end resection. The short single-stranded DNA tails formed in the absence of RPA were unstable due to 3' strand loss and the formation of fold-back hairpin structures that required resection initiation and Pol32-dependent DNA synthesis. Thus, RPA is required to generate ssDNA, and also to protect ssDNA from degradation and inappropriate annealing that could lead to genome rearrangements.
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