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- W2988152034 abstract "Abstract Despite recent evidence suggesting that histone lysine acetylation contributes to base excision repair (BER) in cells, their exact mechanistic role remains unclear. In order to examine the influence of histone acetylation on the initial steps of BER, we assembled nucleosome arrays consisting of homogeneously acetylated histone H3 (H3K18 and H3K27) and measured the repair of a site-specifically positioned 2′-deoxyuridine (dU) residue by uracil DNA glycosylase (UDG) and apurinic/apyrimidinic endonuclease 1 (APE1). We find that H3K18ac and H3K27ac differentially influence the combined activities of UDG/APE1 on compact chromatin, suggesting that acetylated lysine residues on the H3 tail domain play distinct roles in regulating the initial steps of BER. In addition, we show that the effects of H3 tail domain acetylation on UDG/APE1 activity are at the nucleosome level and do not influence higher-order chromatin folding. Overall, these results establish a novel regulatory role for histone H3 acetylation during the initiation of BER on chromatin." @default.
- W2988152034 created "2019-11-22" @default.
- W2988152034 creator A5017205408 @default.
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- W2988152034 date "2019-11-04" @default.
- W2988152034 modified "2023-10-17" @default.
- W2988152034 title "Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures" @default.
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- W2988152034 doi "https://doi.org/10.1038/s41598-019-52340-0" @default.
- W2988152034 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6828659" @default.
- W2988152034 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31685935" @default.
- W2988152034 hasPublicationYear "2019" @default.
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