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Article Dans Une Revue Science Année : 2017

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

Résumé

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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Dates et versions

cea-01588317 , version 1 (15-09-2017)

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Citer

Gilbert Richarme, Cailing Liu, Mouadh Mihoub, Jad Abdallah, Leger Thibaut, et al.. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science, 2017, 357 (6347), pp.208-211. ⟨10.1126/science.aag1095⟩. ⟨cea-01588317⟩
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