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Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation

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dc.contributor.author Zarkovic, Gabriella
dc.contributor.author Belousova, Ekaterina
dc.contributor.author Talhaoui, Ibtissam
dc.contributor.author Saint-Pierre, Christine
dc.contributor.author Kutuzov, Mikhail M.
dc.contributor.author Matkarimov, Bakhyt
dc.contributor.author Biard, Denis
dc.contributor.author Gasparutto, Didier
dc.contributor.author Lavrik, Olga I.
dc.contributor.author Ishchenko, Alexander A.
dc.date.accessioned 2020-03-26T05:32:04Z
dc.date.available 2020-03-26T05:32:04Z
dc.date.issued 2018-01
dc.identifier.citation Zarkovic, G., Belousova, E. A., Talhaoui, I., Saint-Pierre, C., Kutuzov, M. M., Matkarimov, B. T., Biard, D., Gasparutto, D., Lavrik, O. I., & Ishchenko, A. A. (2018). Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation. Nucleic Acids Research, 46(5), 2417–2431. https://doi.org/10.1093/nar/gkx1318 en_US
dc.identifier.issn 0305-1048
dc.identifier.other 1362-4962
dc.identifier.other 10.1093/nar/gkx1318
dc.identifier.uri https://doi.org/10.1093/nar/gkx1318
dc.identifier.uri http://nur.nu.edu.kz/handle/123456789/4544
dc.description https://academic.oup.com/nar/article/46/5/2417/4807332 en_US
dc.description.abstract Poly(ADP-ribose) polymerases (PARPs) act as DNA break sensors and catalyze the synthesis of polymers of ADP-ribose (PAR) covalently attached to acceptor proteins at DNA damage sites. It has been demonstrated that both mammalian PARP1 and PARP2 PARylate double-strand break termini in DNA oligonucleotide duplexes in vitro. Here, we show that mammalian PARP2 and PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5′- and 3′-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks. PARP3-catalyzed DNA MARylation can be considered a new type of reversible post-replicative DNA modification. According to DNA substrate specificity of PARP3 and PARP2, we propose a putative mechanistic model of PARP-catalyzed strand break–oriented ADP-ribosylation of DNA termini. Notably, PARP-mediated DNA ADP-ribosylation can be more effective than PARPs’ auto-ADP-ribosylation depending on the DNA substrates and reaction conditions used. Finally, we show an effective PARP3- or PARP2-catalyzed ADP-ribosylation of high-molecular-weight (∼3-kb) DNA molecules, PARP-mediated DNA PARylation in cell-free extracts and a persisting signal of anti-PAR antibodies in a serially purified genomic DNA from bleomycin-treated poly(ADP-ribose) glycohydrolase-depleted HeLa cells. These results suggest that certain types of complex DNA breaks can be effectively ADP-ribosylated by PARPs in cellular response to DNA damage. en_US
dc.language.iso en en_US
dc.publisher Oxford University Press en_US
dc.relation.ispartofseries Nucleic Acids Research;Vol. 46, No. 5
dc.rights Attribution-NonCommercial-ShareAlike 3.0 United States *
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/us/ *
dc.subject genome integrity en_US
dc.subject repair and replication en_US
dc.subject PARP2 en_US
dc.subject PARP3 en_US
dc.subject Research Subject Categories::MEDICINE en_US
dc.title Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation en_US
dc.type Article en_US
workflow.import.source science

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