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Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro

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dc.contributor.author Talhaoui I. es_PE
dc.contributor.author Lebedeva N.A. es_PE
dc.contributor.author Zarkovic G. es_PE
dc.contributor.author Saint-Pierre C. es_PE
dc.contributor.author Kutuzov M.M. es_PE
dc.contributor.author Sukhanova M.V. es_PE
dc.contributor.author Matkarimov B.T. es_PE
dc.contributor.author Gasparutto D. es_PE
dc.contributor.author Saparbaev M.K. 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 2016
dc.description Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [#306 to A.A.I. and RFBR-16-54-76010 to O.I.L.]; Electricité de France (http://www.edf.fr) [RB 2016-17 to M.K.S.]; Science Committee of the Ministry of Education and Science of the Republic of Kazakhstan (program 0212/PTF-14-OT) [3755/GF4 and 2835/GF3] (http://www.nu.edu.kz) to B.T.M.; RSF [14-24-00038 to O.I.L.]; RFBR [15-54-16003]; Program of RAS on Molecular and Cellular Biology [6.4]; postdoctoral and doctoral fellowships from Fondation ARC (http://www.arc-cancer.net) [PDF20110603195 to I.T. and G.Z.] and CIENCIACTIVA/CONCYTEC (www.cienciactiva.gob.pe), respectively. Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan.
dc.description.abstract Poly(ADP-ribose) polymerases (PARPs/ARTDs) use nicotinamide adenine dinucleotide (NAD+) to catalyse the synthesis of a long branched poly(ADP-ribose) polymer (PAR) attached to the acceptor amino acid residues of nuclear proteins. PARPs act on single- and double-stranded DNA breaks by recruiting DNA repair factors. Here, in in vitro biochemical experiments, we found that the mammalian PARP1 and PARP2 proteins can directly ADP-ribosylate the termini of DNA oligonucleotides. PARP1 preferentially catalysed covalent attachment of ADP-ribose units to the ends of recessed DNA duplexes containing 3′-cordycepin, 5′- and 3′-phosphate and also to 5′-phosphate of a single-stranded oligonucleotide. PARP2 preferentially ADP-ribosylated the nicked/gapped DNA duplexes containing 5′-phosphate at the double-stranded termini. PAR glycohydrolase (PARG) restored native DNA structure by hydrolysing PAR-DNA adducts generated by PARP1 and PARP2. Biochemical and mass spectrometry analyses of the adducts suggested that PARPs utilise DNA termini as an alternative to 2′-hydroxyl of ADP-ribose and protein acceptor residues to catalyse PAR chain initiation either via the 2′,1″-O-glycosidic ribose-ribose bond or via phosphodiester bond formation between C1′ of ADP-ribose and the phosphate of a terminal deoxyribonucleotide. This new type of post-replicative modification of DNA provides novel insights into the molecular mechanisms underlying biological phenomena of ADP-ribosylation mediated by PARPs.
dc.description.sponsorship Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica - Concytec
dc.identifier.doi https://doi.org/10.1093/nar/gkw675
dc.identifier.scopus 2-s2.0-84994817680
dc.identifier.uri https://hdl.handle.net/20.500.12390/742
dc.language.iso eng
dc.publisher Oxford University Press
dc.relation.ispartof Nucleic Acids Research
dc.rights info:eu-repo/semantics/openAccess
dc.rights.uri http://creativecommons.org/licenses/by-nc/4.0/
dc.subject monomer
dc.subject cordycepin es_PE
dc.subject DNA fragment es_PE
dc.subject double stranded DNA es_PE
dc.subject glycosidase es_PE
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#1.04.00
dc.title Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro
dc.type info:eu-repo/semantics/article
dspace.entity.type Publication
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