Система будет остановлена для регулярного обслуживания. Пожалуйста, сохраните рабочие данные и выйдите из системы.
dc.contributor.author | Talhaoui, Ibtissam![]() |
|
dc.contributor.author | Lebedeva, Natalia A.![]() |
|
dc.contributor.author | Zarkovic, Gabriella![]() |
|
dc.contributor.author | Saint-Pierre, Christine![]() |
|
dc.contributor.author | Kutuzov, Mikhail M.![]() |
|
dc.contributor.author | Sukhanova, Maria V.![]() |
|
dc.contributor.author | Matkarimov, Bakhyt T.![]() |
|
dc.contributor.author | Gasparutto, Didier![]() |
|
dc.contributor.author | Saparbaev, Murat K.![]() |
|
dc.contributor.author | Lavrik, Olga I.![]() |
|
dc.contributor.author | Ishchenko, Alexander A.![]() |
|
dc.date.accessioned | 2017-11-14T08:39:02Z | |
dc.date.available | 2017-11-14T08:39:02Z | |
dc.date.issued | 2016-07-28 | |
dc.identifier.citation | Talhaoui Ibtissam et al.(>10), 2016(July 28), Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro, Nucleic Acids Research, Vol.44, No.19 | ru_RU |
dc.identifier.issn | 9279–9295 | |
dc.identifier.uri | doi: 10.1093/nar/gkw675 | |
dc.identifier.uri | http://nur.nu.edu.kz/handle/123456789/2809 | |
dc.description.abstract | Poly(ADP-ribose) polymerases (PARPs/ARTDs) use nicotinamide adenine dinucleotide (NAD+) to catalyse the synthesis of a long branched poly(ADPribose) 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 singlestranded oligonucleotide. PARP2 preferentially ADPribosylated 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 ADPribose 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. | ru_RU |
dc.language.iso | en | ru_RU |
dc.publisher | Nucleic Acids Research | ru_RU |
dc.rights | Open Access - the content is available to the general public | ru_RU |
dc.rights | Attribution-NonCommercial-ShareAlike 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/3.0/us/ | * |
dc.subject | polymerases | ru_RU |
dc.subject | nicotinamide adenine dinucleotide | ru_RU |
dc.subject | nuclear proteins | ru_RU |
dc.subject | DNA | ru_RU |
dc.subject | PAR | ru_RU |
dc.subject | PARP | ru_RU |
dc.title | Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro | ru_RU |
dc.type | Article | ru_RU |
The following license files are associated with this item: