Acetylation blocks DNA damage-induced chromatin ADP-ribosylation

Nature Chemical Biology
Glen LiszczakTom W Muir

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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Citations

Apr 18, 2019·Open Biology·Luca PalazzoIvan Ahel
Nov 19, 2019·Proteomics·Gregory TomblineVera Gorbunova
Jun 13, 2020·SLAS Discovery·Sarah WazirLari Lehtiö
Aug 14, 2020·Chembiochem : a European Journal of Chemical Biology·Jenna N BeyerGeorge M Burslem
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Jul 16, 2021·Journal of the American Chemical Society·Nir HananyaTom W Muir
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Jul 30, 2021·Communications Biology·Antonio Ginés García-SauraHerwig Schüler
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Sep 7, 2021·Frontiers in Cellular and Infection Microbiology·Tianshu SunYingchun Xu
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Jan 15, 2022·Nature Communications·Julien BrustelNicholas D Lakin

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Methods Mentioned

BETA
acetylation
histone acetylation
protein folding
transfection
PCR
immunoprecipitation
gel filtration
electrophoresis
pull down
transfections

Software Mentioned

R
GraphPad Prism
GENEWIZ
GALAXY

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