Dataset Information

PARP1 exhibits enhanced association and catalytic efficiency with ?H2A.X-nucleosome.

ABSTRACT: The poly(ADP-ribose) polymerase, PARP1, plays a key role in maintaining genomic integrity by detecting DNA damage and mediating repair. ?H2A.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 (?)H2A.X- versus H2A-nucleosomes, resulting in a higher affinity for the former, which is maximal for ?H2A.X-nucleosome that is also the activator eliciting the greatest poly-ADP-ribosylation catalytic efficiency. The enhanced activities with ?H2A.X-nucleosome coincide with increased accessibility of the DNA termini resulting from the H2A.X-Ser139 phosphorylation. Indeed, H2A- and (?)H2A.X-nucleosomes have distinct stability characteristics, which are rationalized by mutational analysis and (?)H2A.X-nucleosome core crystal structures. This suggests that the ?H2A.X epigenetic marker directly facilitates DNA repair by stabilizing PARP1 association and promoting catalysis.

SUBMITTER: Sharma D

PROVIDER: S-EPMC6917767 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome.

Sharma Deepti D De Falco Louis L Padavattan Sivaraman S Rao Chang C Geifman-Shochat Susana S Liu Chuan-Fa CF Davey Curt A CA

Nature communications 20191217 1

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-nucleoso ...[more]

PMID: 31848352

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Dataset Information

PARP1 exhibits enhanced association and catalytic efficiency with ?H2A.X-nucleosome.

Publications

PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome.

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