Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)837-840
Number of pages4
JournalNature chemical biology
Volume14
Issue number9
DOIs
StatePublished - Sep 1 2018
Externally publishedYes

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Acetylation
Adenosine Diphosphate
Serine
DNA Damage
Chromatin
Histone Code
Histone Deacetylase Inhibitors
Nucleosomes
DNA
Histones
Neoplasms
Poly(ADP-ribose) Polymerase Inhibitors

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Acetylation blocks DNA damage–induced chromatin ADP-ribosylation. / Liszczak, Glen; Diehl, Katharine L.; Dann, Geoffrey P.; Muir, Tom W.

In: Nature chemical biology, Vol. 14, No. 9, 01.09.2018, p. 837-840.

Research output: Contribution to journalArticle

Liszczak, Glen ; Diehl, Katharine L. ; Dann, Geoffrey P. ; Muir, Tom W. / Acetylation blocks DNA damage–induced chromatin ADP-ribosylation. In: Nature chemical biology. 2018 ; Vol. 14, No. 9. pp. 837-840.
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