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

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
    • Publication Information:
      Publication: <2002- >: San Diego, CA : Elsevier
      Original Publication: New York, Academic Press.
    • Subject Terms:
      Escherichia coli/*metabolism ; Escherichia coli Proteins/*metabolism ; Glyoxal/*metabolism ; Heat-Shock Proteins/*metabolism ; Molecular Chaperones/*metabolism ; Pyruvaldehyde/*metabolism ; Ribosomal Proteins/*metabolism; Cytoprotection/physiology ; Glycation End Products, Advanced/metabolism
    • 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.
      (Copyright © 2016 Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Carbonyl stress; Electrophile stress; Glycation; Maillard reaction; Protein repair
    • Accession Number:
      0 (Escherichia coli Proteins)
      0 (Glycation End Products, Advanced)
      0 (Heat-Shock Proteins)
      0 (Molecular Chaperones)
      0 (Ribosomal Proteins)
      0 (YajL protein, E coli)
      0 (YhbO protein, E coli)
      0 (hchA protein, E coli)
      50NP6JJ975 (Glyoxal)
      722KLD7415 (Pyruvaldehyde)
    • Publication Date:
      Date Created: 20160118 Date Completed: 20160614 Latest Revision: 20220408
    • Publication Date:
      20250114
    • Accession Number:
      10.1016/j.bbrc.2016.01.068
    • Accession Number:
      26774339