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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Belousova EA,Ishchenko АA,Lavrik OIdoi
10.1038/s41598-018-22673-3subject
Has Abstractpub_date
2018-03-08 00:00:00pages
4176issue
1issn
2045-2322pii
10.1038/s41598-018-22673-3journal_volume
8pub_type
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