DNA is a New Target of Parp3

E. A. Belousova, A. A. Ishchenko, O. I. Lavrik

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

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 languageEnglish
Article number4176
Pages (from-to)4176
Number of pages12
JournalScientific Reports
Volume8
Issue number1
DOIs
Publication statusPublished - 8 Mar 2018

Keywords

  • 3P21.3
  • CELLULAR-RESPONSE
  • CLONING
  • DAMAGE
  • EXPRESSION
  • GENES
  • POLY(ADP-RIBOSE) POLYMERASES
  • PROGRESSION
  • PROTEIN ADP-RIBOSYLATION
  • STRAND BREAKS

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