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Mol. Cells 2010; 29(2): 145-151

Published online February 28, 2010

https://doi.org/10.1007/s10059-010-0023-1

© The Korean Society for Molecular and Cellular Biology

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 Wi1, Hyun Suk Jung2, Woojun Park3, and Byung Yeoup Chung*

Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup 580-185, Korea, 1Bio-Energy Research Institute, Chonnam National University, Gwangju 500-757, Korea, 2Division of Electron Microscopic Research, Korea Basic Science Institute, Daejeon 305-333, Korea, 3Division of Environmental Sciences and Ecological Engineering, Korea University, Seoul 136-701, Korea

Correspondence to : *Correspondence: bychung@kaeri.re.kr

Received: August 5, 2009; Revised: October 29, 2009; Accepted: November 3, 2009

Abstract

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 glu-tathione (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.

Keywords chaperone, oxidative stress, peroxidase, peroxiredoxin, Pseudomonas aeruginosa

Article

Research Article

Mol. Cells 2010; 29(2): 145-151

Published online February 28, 2010 https://doi.org/10.1007/s10059-010-0023-1

Copyright © The Korean Society for Molecular and Cellular Biology.

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 Wi1, Hyun Suk Jung2, Woojun Park3, and Byung Yeoup Chung*

Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup 580-185, Korea, 1Bio-Energy Research Institute, Chonnam National University, Gwangju 500-757, Korea, 2Division of Electron Microscopic Research, Korea Basic Science Institute, Daejeon 305-333, Korea, 3Division of Environmental Sciences and Ecological Engineering, Korea University, Seoul 136-701, Korea

Correspondence to:*Correspondence: bychung@kaeri.re.kr

Received: August 5, 2009; Revised: October 29, 2009; Accepted: November 3, 2009

Abstract

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 glu-tathione (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.

Keywords: chaperone, oxidative stress, peroxidase, peroxiredoxin, Pseudomonas aeruginosa

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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