PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2BGlu2

Gabrielle J. Grundy, Luis M. Polo, Zhihong Zeng, Stuart L. Rulten, Nicolas C. Hoch, Pathompong Paomephan, Yingqi Xu, Steve M. Sweet, Alan W. Thorne, Antony W. Oliver, Steve J. Matthews, Laurence H. Pearl and Keith W. Caldecott ()
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Gabrielle J. Grundy: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Luis M. Polo: Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Zhihong Zeng: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Stuart L. Rulten: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Nicolas C. Hoch: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Pathompong Paomephan: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Yingqi Xu: Cross-faculty NMR centre, Faculty of Natural Sciences, Imperial College London
Steve M. Sweet: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Alan W. Thorne: Institute of Biomedical and Biomolecular Sciences, University of Portsmouth
Antony W. Oliver: Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Steve J. Matthews: Cross-faculty NMR centre, Faculty of Natural Sciences, Imperial College London
Laurence H. Pearl: Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Keith W. Caldecott: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract PARP3 is a member of the ADP-ribosyl transferase superfamily that we show accelerates the repair of chromosomal DNA single-strand breaks in avian DT40 cells. Two-dimensional nuclear magnetic resonance experiments reveal that PARP3 employs a conserved DNA-binding interface to detect and stably bind DNA breaks and to accumulate at sites of chromosome damage. PARP3 preferentially binds to and is activated by mononucleosomes containing nicked DNA and which target PARP3 trans-ribosylation activity to a single-histone substrate. Although nicks in naked DNA stimulate PARP3 autoribosylation, nicks in mononucleosomes promote the trans-ribosylation of histone H2B specifically at Glu2. These data identify PARP3 as a molecular sensor of nicked nucleosomes and demonstrate, for the first time, the ribosylation of chromatin at a site-specific DNA single-strand break.

Date: 2016
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DOI: 10.1038/ncomms12404

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