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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 G. es_PE
dc.contributor.author Belousova E.A. es_PE
dc.contributor.author Talhaoui I. es_PE
dc.contributor.author Saint-Pierre C. es_PE
dc.contributor.author Kutuzov M.M. es_PE
dc.contributor.author Matkarimov B.T. es_PE
dc.contributor.author Biard D. es_PE
dc.contributor.author Gasparutto D. es_PE
dc.contributor.author Lavrik O.I. es_PE
dc.contributor.author Ishchenko A.A. es_PE
dc.date.accessioned 2024-05-30T23:13:38Z
dc.date.available 2024-05-30T23:13:38Z
dc.date.issued 2018
dc.description Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [DNA PARYLATION #306 to A.A.I., RFBR-16–54-76010 to O.I.L.]; Ministry of Education and Science of the Republic of Kazakhstan [programs 0115RK02473 and 0115RK03029 to B.T.M.]; NU ORAU (http://www.nu.edu.kz) (to B.T.M.); RSF Grant [14–24-00038 to O.I.L.]; French National Research Agency ‘Labex program’ [ARCANE project ANR-11-LABX-0003–01 to C.S.-P., D.G.]; Fondation ARC Postdoctoral Fellowship (http://www.arc-cancer.net) [PDF20110603195 to I.T.]; CIENCIACTIVA/CONCYTEC Doctoral Fellowship (www.cienciactiva.gob.pe) (to G.Z.). Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan.
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.
dc.description.sponsorship Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica - Concytec
dc.identifier.doi https://doi.org/10.1093/nar/gkx1318
dc.identifier.scopus 2-s2.0-85043399955
dc.identifier.uri https://hdl.handle.net/20.500.12390/549
dc.language.iso eng
dc.publisher Oxford University Press
dc.relation.ispartof Nucleic Acids Research
dc.rights info:eu-repo/semantics/openAccess
dc.subject unclassified drug
dc.subject bleomycin es_PE
dc.subject DNA es_PE
dc.subject genomic DNA es_PE
dc.subject glycosidase es_PE
dc.subject nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase es_PE
dc.subject nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2 es_PE
dc.subject nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3 es_PE
dc.subject poly(adenosine diphosphate ribose) es_PE
dc.subject Article es_PE
dc.subject cell free system es_PE
dc.subject controlled study es_PE
dc.subject DNA damage es_PE
dc.subject DNA modification es_PE
dc.subject DNA replication es_PE
dc.subject double stranded DNA break es_PE
dc.subject enzyme active site es_PE
dc.subject enzyme activity es_PE
dc.subject enzyme mechanism es_PE
dc.subject enzyme specificity es_PE
dc.subject HeLa cell line es_PE
dc.subject human es_PE
dc.subject human cell es_PE
dc.subject molecular weight es_PE
dc.subject mono adenosine diphosphate ribosylation es_PE
dc.subject priority journal es_PE
dc.subject single stranded DNA break es_PE
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.01.02
dc.title Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
dc.type info:eu-repo/semantics/article
dspace.entity.type Publication
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