Literature DB >> 30013063

Acetylation blocks DNA damage-induced chromatin ADP-ribosylation.

Glen Liszczak1, Katharine L Diehl1, Geoffrey P Dann1, Tom W Muir2.   

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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Year:  2018        PMID： 30013063      PMCID： PMC6505472          DOI： 10.1038/s41589-018-0097-1

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


  31 in total

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7.  Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.

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8.  Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.

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Review 9.  Sirtuin 6: linking longevity with genome and epigenome stability.

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Review 10.  PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.

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