Insight into DNA substrate specificity of PARP1-catalysed DNA poly(ADP-ribosyl)ation

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dc.contributor.authorElie Matta
dc.date.accessioned2025-08-19T12:40:14Z
dc.date.available2025-08-19T12:40:14Z
dc.date.issued2020-01-01
dc.description.abstractThis study investigates how PARP1 recognizes and PARylates various DNA duplex substrates with different types and positions of strand breaks. The authors found that PARP1 preferentially attaches ADP-ribose moieties to 3′-terminal phosphate residues at double-strand break ends, influenced by the orientation and spacing of DNA strand breaks on the same molecule. This preference surpasses PARP1 self-PARylation and holds both for purified recombinant PARP1 and HeLa cell extracts, suggesting that in vivo DNA modification by PARP1 strongly depends on DNA break configuration., en
dc.identifier.citationMatta E, Kiribayeva A, Khassenov B, Matkarimov BT, Ishchenko AA (2020). Insight into DNA substrate specificity of PARP1-catalysed DNA poly(ADP-ribosyl)ation. Scientific Reports, 10(1):3699. doi:10.1038/s41598-020-60631-0 en
dc.identifier.doi10.1038/s41598-020-60631-0
dc.identifier.urihttps://doi.org/10.1038/s41598-020-60631-0
dc.identifier.urihttps://nur.nu.edu.kz/handle/123456789/9630
dc.language.isoen
dc.publisherNature Portfolio
dc.relation.ispartofScientific Reportsen
dc.rightsOpen accessen
dc.sourceScientific Reports, 10, (2020)en
dc.subjectPARP1, DNA PARylation, substrate specificity, 3′-terminal phosphate, DNA breaks, PARP1-mediated DNA modificationen
dc.titleInsight into DNA substrate specificity of PARP1-catalysed DNA poly(ADP-ribosyl)ationen
dc.typeJournal Articleen

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