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- W2793735223 abstract "Abstract Dna2 is a nuclease and helicase that functions redundantly with other proteins in Okazaki fragment processing, double-strand break resection, and checkpoint kinase activation. Dna2 is an essential enzyme, required for yeast and mammalian cell viability. Here, we report that numerous mutations affecting the DNA damage checkpoint suppress dna2∆ lethality in Saccharomyces cerevisiae. dna2∆ cells are also suppressed by deletion of helicases PIF1 and MPH1, and by deletion of POL32, a subunit of DNA polymerase δ. All dna2∆ cells are temperature sensitive, have telomere length defects, and low levels of telomeric 3′ single-stranded DNA (ssDNA). Interestingly, Rfa1, a subunit of the major ssDNA binding protein RPA, and the telomere-specific ssDNA binding protein Cdc13, often colocalize in dna2∆ cells. This suggests that telomeric defects often occur in dna2∆ cells. There are several plausible explanations for why the most critical function of Dna2 is at telomeres. Telomeres modulate the DNA damage response at chromosome ends, inhibiting resection, ligation, and cell-cycle arrest. We suggest that Dna2 nuclease activity contributes to modulating the DNA damage response at telomeres by removing telomeric C-rich ssDNA and thus preventing checkpoint activation." @default.
- W2793735223 created "2018-03-29" @default.
- W2793735223 creator A5026274019 @default.
- W2793735223 creator A5053272751 @default.
- W2793735223 creator A5078694198 @default.
- W2793735223 date "2018-03-20" @default.
- W2793735223 modified "2023-10-13" @default.
- W2793735223 title "A Critical Role for Dna2 at Unwound Telomeres" @default.
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- W2793735223 doi "https://doi.org/10.1534/genetics.118.300809" @default.
- W2793735223 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5937186" @default.
- W2793735223 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29559500" @default.
- W2793735223 hasPublicationYear "2018" @default.
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