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- W2404455434 abstract "To allow for sufficient time to repair DNA double-stranded breaks (DSBs), eukaryotic cells activate the DNA damage checkpoint. In budding yeast, Rad53 (mammalian Chk2) phosphorylation parallels the persistence of the unrepaired DSB and is extinguished when repair is complete in a process termed recovery or when the cells adapt to the DNA damage checkpoint. A strain containing a slowly repaired DSB does not require the histone chaperone Asf1 to resume cell cycle progression after DSB repair. When a second, rapidly repairable DSB is added to this strain, Asf1 becomes required for recovery. Recovery from two repairable DSBs also depends on the histone acetyltransferase Rtt109 and the cullin subunit Rtt101, both of which modify histone H3 that is associated with Asf1. We show that dissociation of histone H3 from Asf1 is required for efficient recovery and that Asf1 is required for complete dephosphorylation of Rad53 when the upstream DNA damage checkpoint signaling is turned off. Our data suggest that the requirements for recovery from the DNA damage checkpoint become more stringent with increased levels of damage and that Asf1 plays a histone chaperone-independent role in facilitating complete Rad53 dephosphorylation following repair." @default.
- W2404455434 created "2016-06-24" @default.
- W2404455434 creator A5001037106 @default.
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- W2404455434 creator A5085085286 @default.
- W2404455434 date "2016-05-15" @default.
- W2404455434 modified "2023-10-17" @default.
- W2404455434 title "Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair" @default.
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- W2404455434 doi "https://doi.org/10.1101/gad.280685.116" @default.
- W2404455434 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4888841" @default.
- W2404455434 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27222517" @default.
- W2404455434 hasPublicationYear "2016" @default.
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