A new antioxidant with dual functions as a peroxidase and chaperone in Pseudomonas aeruginosa

Byung Chull An, Seung Sik Lee, Eun Mi Lee, Jae Taek Lee, Seung Gon Wi, Hyun Suk Jung, Woojun Park, Byung Yeoup Chung

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


Thiol-based peroxiredoxins (Prxs) are conserved throughout all kingdoms. We have found that a conserved typical 2-Cys Prx-like protein (PaPrx) from Pseudomonas aeruginosa bacteria displays diversity in its structure and apparent molecular weight (MW), and can act alternatively as a peroxidase and molecular chaperone. We have also identified a regulatory factor involved in this structural and functional switching. Exposure of P. aeruginosa to hydrogen peroxide (H2O2) causes PaPrx to convert from a high MW (HMW) complex to a low MW (LMW) form, which triggers a chaperone to peroxidase functional switch. This structural switching is primarily guided by either the thioredoxin (Trx) or glutathione (GSH) systems. Furthermore, comparison of our structural data [native and non-reducing polyacrylamide gel electrophoresis (PAGE) analysis, size exclusion chromatography (SEC) analysis, and electron microscopy (EM) observations] and enzymatic analyses (peroxidase and chaperone assay) revealed that the formation of oligomeric HMW complex structures increased chaperone activity of PaPrx. These results suggest that multimerization of PaPrx complexes promotes chaperone activity, and dissociation of the complexes into LMW species enhances peroxidase activity. Thus, the dual functions of PaPrx are clearly associated with their ability to form distinct protein structures.

Original languageEnglish
Pages (from-to)145-151
Number of pages7
JournalMolecules and cells
Issue number2
Publication statusPublished - 2010 Feb


  • Chaperone
  • Oxidative stress
  • Peroxidase
  • Peroxiredoxin
  • Pseudomonas aeruginosa

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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