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Nat Chem Biol. 2018 Sep;14(9):837-840. doi: 10.1038/s41589-018-0097-1. Epub 2018 Jul 16.

Acetylation blocks DNA damage-induced chromatin ADP-ribosylation.

Author information

1
Department of Chemistry, Princeton University, Princeton, NJ, USA.
2
Department of Chemistry, Princeton University, Princeton, NJ, USA. muir@princeton.edu.

Abstract

Recent studies report serine ADP-ribosylation on nucleosomes during the DNA damage response. We unveil histone H3 serine 10 as the primary acceptor residue for chromatin ADP-ribosylation and find that specific histone acetylation marks block this activity. Our results provide a molecular explanation for the well-documented phenomenon of rapid deacetylation at DNA damage sites and support the combinatorial application of PARP and HDAC inhibitors for the treatment of PARP-dependent cancers.

PMID:
30013063
DOI:
10.1038/s41589-018-0097-1

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