Guanine glycation repair by DJ-1/Park7 and its bacterial homologs

Abstract : DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair, how glycated DNA is repaired remains undetermined. Here, we found that the parkinsonism-associated protein DJ-1 and its bacterial homologs Hsp31, YhbO, and YajL could repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids. DJ-1–depleted cells displayed increased levels of glycated DNA, DNA strand breaks, and phosphorylated p53. Deglycase-deficient bacterial mutants displayed increased levels of glycated DNA and RNA and exhibited strong mutator phenotypes. Thus, DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that we name guanine glycation repair.
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Science, American Association for the Advancement of Science, 2017, 357 (6347), pp.208-211. 〈http://science.sciencemag.org/content/357/6347/208/tab-article-info〉. 〈10.1126/science.aag1095〉
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https://hal-cea.archives-ouvertes.fr/cea-01588317
Contributeur : Quentin Jaillard <>
Soumis le : vendredi 15 septembre 2017 - 14:46:04
Dernière modification le : vendredi 27 juillet 2018 - 11:16:02

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Richarme Gilbert, Liu Cailing, Mihoub1 Mouadh, Abdallah Jad, Leger Thibaut, et al.. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science, American Association for the Advancement of Science, 2017, 357 (6347), pp.208-211. 〈http://science.sciencemag.org/content/357/6347/208/tab-article-info〉. 〈10.1126/science.aag1095〉. 〈cea-01588317〉

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