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- W2996208548 abstract "Abstract The poly(ADP-ribose) polymerase, PARP1, plays a key role in maintaining genomic integrity by detecting DNA damage and mediating repair. γH2A.X is the primary histone marker for DNA double-strand breaks and PARP1 localizes to H2A.X-enriched chromatin damage sites, but the basis for this association is not clear. We characterize the kinetics of PARP1 binding to a variety of nucleosomes harbouring DNA double-strand breaks, which reveal that PARP1 associates faster with (γ)H2A.X- versus H2A-nucleosomes, resulting in a higher affinity for the former, which is maximal for γH2A.X-nucleosome that is also the activator eliciting the greatest poly-ADP-ribosylation catalytic efficiency. The enhanced activities with γH2A.X-nucleosome coincide with increased accessibility of the DNA termini resulting from the H2A.X-Ser139 phosphorylation. Indeed, H2A- and (γ)H2A.X-nucleosomes have distinct stability characteristics, which are rationalized by mutational analysis and (γ)H2A.X-nucleosome core crystal structures. This suggests that the γH2A.X epigenetic marker directly facilitates DNA repair by stabilizing PARP1 association and promoting catalysis." @default.
- W2996208548 created "2019-12-26" @default.
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- W2996208548 date "2019-12-17" @default.
- W2996208548 modified "2023-10-13" @default.
- W2996208548 title "PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome" @default.
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- W2996208548 doi "https://doi.org/10.1038/s41467-019-13641-0" @default.
- W2996208548 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6917767" @default.
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