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 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 language | English |
|---|---|
| Pages (from-to) | 145-151 |
| Number of pages | 7 |
| Journal | Molecules and Cells |
| Volume | 29 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2010 Feb 1 |
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Keywords
- Chaperone
- Oxidative stress
- Peroxidase
- Peroxiredoxin
- Pseudomonas aeruginosa
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
A new antioxidant with dual functions as a peroxidase and chaperone in Pseudomonas aeruginosa. / An, Byung Chull; Lee, Seung Sik; Lee, Eun Mi; Lee, Jae Taek; Wi, Seung Gon; Jung, Hyun Suk; Park, Woojun; Chung, Byung Yeoup.
In: Molecules and Cells, Vol. 29, No. 2, 01.02.2010, p. 145-151.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A new antioxidant with dual functions as a peroxidase and chaperone in Pseudomonas aeruginosa
AU - An, Byung Chull
AU - Lee, Seung Sik
AU - Lee, Eun Mi
AU - Lee, Jae Taek
AU - Wi, Seung Gon
AU - Jung, Hyun Suk
AU - Park, Woojun
AU - Chung, Byung Yeoup
PY - 2010/2/1
Y1 - 2010/2/1
N2 - 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.
AB - 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.
KW - Chaperone
KW - Oxidative stress
KW - Peroxidase
KW - Peroxiredoxin
KW - Pseudomonas aeruginosa
UR - http://www.scopus.com/inward/record.url?scp=77949424963&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77949424963&partnerID=8YFLogxK
U2 - 10.1007/s10059-010-0023-1
DO - 10.1007/s10059-010-0023-1
M3 - Article
C2 - 20082221
AN - SCOPUS:77949424963
VL - 29
SP - 145
EP - 151
JO - Molecules and Cells
JF - Molecules and Cells
SN - 1016-8478
IS - 2
ER -