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.
Original language | English |
---|---|
Article number | 4176 |
Pages (from-to) | 4176 |
Number of pages | 12 |
Journal | Scientific Reports |
Volume | 8 |
Issue number | 1 |
DOIs | |
Publication status | Published - 8 Mar 2018 |
Keywords
- 3P21.3
- CELLULAR-RESPONSE
- CLONING
- DAMAGE
- EXPRESSION
- GENES
- POLY(ADP-RIBOSE) POLYMERASES
- PROGRESSION
- PROTEIN ADP-RIBOSYLATION
- STRAND BREAKS