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.
Original language | English (US) |
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Pages (from-to) | 837-840 |
Number of pages | 4 |
Journal | Nature Chemical Biology |
Volume | 14 |
Issue number | 9 |
DOIs | |
State | Published - Sep 1 2018 |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology