Parkinsonism-associated protein DJ-1 is a bona fide deglycase
- Biochem Biophys Res Commun. 2017 Jan 29;483(1):387-391. doi: 10.1016/j.bbrc.2016.12.134.
- 1. Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 Rue Hélène Brion, 75013, Paris, France. Electronic address: [email protected].
- 2. UMR 8601 CNRS, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, Université Paris Descartes-Sorbonne Paris Cité, 75270, Paris, France.
We discovered recently that Parkinsonism-associated DJ-1 and its Bacterial homologs function as protein deglycases that repair glyoxal- and methylglyoxal-glycated proteins. Protein glycation levels are 2- to 10-fold increased in deglycase-depleted cells, and deglycase mutants display up to 500-fold loss of viability in methylglyoxal or glucose-containing media, suggesting that these deglycases play important roles in protecting cells against electrophile and carbonyl stress. Although the deglycase activity of DJ-1 is well supported by extensive biochemical work, Pfaff et al. (J. Biol. Chem. in presshttp://dx.doi.org/10.1074/jbc.M116.743823) claimed in a recent study that deglycation of the hemithioacetal formed upon cysteine glycation by methylglyoxal results from a Tris buffer artefact. Here, we show that this is not the case, and that DJ-1 and its homologs are the bona fide deglycases awaited since the Maillard discovery.