University of Sussex
Browse
- No file added yet -

PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2B(Glu2)

Download (3.09 MB)
journal contribution
posted on 2023-06-09, 02:39 authored by Gabrielle J Grundy, Luis M Polo, Zhihong Zeng, Stuart L Rulten, Nicolas C Hoch, Paomephan Pathompong, Yingqi Xu, Steve M Sweet, Alan W Thorne, Antony OliverAntony Oliver, Steve J Matthews, Laurence PearlLaurence Pearl, Keith CaldecottKeith Caldecott
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.

History

Publication status

  • Published

File Version

  • Published version

Journal

Nature Communications

ISSN

2041-1723

Publisher

Nature Publishing Group

Issue

1

Volume

7

Page range

1-12

Article number

a12404

Department affiliated with

  • Sussex Centre for Genome Damage Stability Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2016-08-26

First Open Access (FOA) Date

2016-08-26

First Compliant Deposit (FCD) Date

2016-08-26

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Licence

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC