Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

Glen Liszczak; Katharine L. Diehl; Geoffrey P. Dann; Tom W. Muir

doi:10.1038/s41589-018-0097-1

Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

Glen Liszczak
, Katharine L. Diehl
, Geoffrey P. Dann
, Tom W. Muir

Research output: Contribution to journal › Article › peer-review

76 Scopus citations

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)
Pages (from-to)	837-840
Number of pages	4
Journal	Nature Chemical Biology
Volume	14
Issue number	9
DOIs	https://doi.org/10.1038/s41589-018-0097-1
State	Published - Sep 1 2018

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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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.",

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AB - 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.

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Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

Abstract

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