The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal

Biochem Biophys Res Commun. 2016 Feb 5;470(2):282-286. doi: 10.1016/j.bbrc.2016.01.068. Epub 2016 Jan 14.

Abstract

YhbO and YajL belong to the PfpI/Hsp31/DJ-1 superfamily. Both proteins are involved in protection against environmental stresses. Here, we show that, like DJ-1 and Hsp31, they repair glyoxal- and methylglyoxal-glycated proteins. YhbO and YajL repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. Moreover, yhbO and yajL mutants display decreased viability in methylglyoxal- or glucose-containing media. Finally, the apparent glyoxalase activities of YhbO and YajL reflect their deglycase activities.

Keywords: Carbonyl stress; Electrophile stress; Glycation; Maillard reaction; Protein repair.

MeSH terms

  • Cytoprotection / physiology
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Glycation End Products, Advanced / metabolism
  • Glyoxal / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Molecular Chaperones / metabolism*
  • Pyruvaldehyde / metabolism*
  • Ribosomal Proteins / metabolism*

Substances

  • Escherichia coli Proteins
  • Glycation End Products, Advanced
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Ribosomal Proteins
  • YajL protein, E coli
  • YhbO protein, E coli
  • hchA protein, E coli
  • Glyoxal
  • Pyruvaldehyde