title: The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal.
abstract: Hsp31 belongs to the PfpI/Hsp31/DJ-1 superfamily, and has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities. Here, we show that Hsp31 repairs glyoxal- and methylglyoxal-glycated amino acids and proteins and releases repaired proteins and lactate or glycolate, respectively. Hsp31 deglycates cysteine, arginine and lysine by acting on early glycation intermediates (hemithioacetals and aminocarbinols) and prevents the formation of Schiff bases and advanced glycation endproducts. Hsp31 repairs glycated serum albumin, glyceraldehyde-3-phosphate dehydrogenase, fructose biphosphate aldolase and aspartate aminotransferase. Moreover, we show that bacterial extracts from the hchA mutant display increased glycation levels and that the apparent glyoxalase activity of Hsp31 reflects its deglycase activity. Our results suggest that other Hsp31 members, previously characterized as glutathione-independent glyoxalases, likely function as protein deglycases.
authors.affiliation: Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 Rue Hélène Brion, 75013 Paris, France.
authors.forename: Mouadh
authors.initials: M
authors.lastname: Mihoub
authors.affiliation: Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 Rue Hélène Brion, 75013 Paris, France.
authors.forename: Jad
authors.initials: J
authors.lastname: Abdallah
authors.affiliation: UMR 7281, CNRS, Aix-Marseille Université Marseille, France.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Gontero
authors.affiliation: Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 Rue Hélène Brion, 75013 Paris, France.
authors.forename: Julien
authors.initials: J
authors.lastname: Dairou
authors.affiliation: Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 15 Rue Hélène Brion, 75013 Paris, France. Electronic address: richarme@paris7.jussieu.fr.
authors.forename: Gilbert
authors.initials: G
authors.lastname: Richarme
mesh_terms: D001120:Arginine / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000502:physiology*; D005947:Glucose / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006037:Glyoxal / Q000494:pharmacology*; D008239:Lysine / Q000378:metabolism; D018832:Molecular Chaperones / Q000502:physiology*; D011765:Pyruvaldehyde / Q000494:pharmacology*; D012545:Schiff Bases
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D012545:Schiff Bases; C469996:hchA protein, E coli; D006037:Glyoxal; D011765:Pyruvaldehyde; D001120:Arginine; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005947:Glucose; D008239:Lysine; D003545:Cysteine
keywords: Advanced glycation endproducts; Carbonyl stress; Electrophile stress; Glycation; Maillard reaction; Protein repair