Dna is a New Target of Parp3

Sci Rep. 2018 Mar 8;8(1):4176. doi: 10.1038/s41598-018-22673-3.

E A Belousova ¹, А A Ishchenko ² ³, O I Lavrik ⁴ ⁵

Affiliations

1 Institute of Chemical Biology and Fundamental Medicine (ICBFM), SB RAS, Lavrentiev Av. 8, Novosibirsk, 630090, Russia.
2 Groupe Réparation de l'ADN, Equipe Labellisée par la Ligue Nationale Contre le Cancer, CNRS UMR8200, Univ. Paris-Sud, Université Paris-Saclay, F-94805, Villejuif, France.
3 Gustave Roussy, Université Paris-Saclay, F-94805, Villejuif, France.
4 Institute of Chemical Biology and Fundamental Medicine (ICBFM), SB RAS, Lavrentiev Av. 8, Novosibirsk, 630090, Russia. lavrik@niboch.nsc.ru.
5 Novosibirsk State University, Pirogov Str. 2, Novosibirsk, 630090, Russia. lavrik@niboch.nsc.ru.

PMID: 29520010 DOI: 10.1038/s41598-018-22673-3

Abstract

Most members of the poly(ADP-ribose)polymerase family, PARP family, have a catalytic activity that involves the transfer of ADP-ribose from a beta-NAD+-molecule to protein acceptors. It was recently discovered by Talhaoui et al. that DNA-dependent PARP1 and PARP2 can also modify DNA. Here, we demonstrate that DNA-dependent PARP3 can modify DNA and form a specific primed structure for further use by the repair proteins. We demonstrated that gapped DNA that was ADP-ribosylated by PARP3 could be ligated to double-stranded DNA by DNA ligases. Moreover, this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts. We suggest that this ADP-ribose modification can be involved in cellular pathways that are important for cell survival in the process of double-strand break formation.

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