Functional switching of a novel prokaryotic 2-Cys peroxiredoxin (PpPrx) under oxidative stress |
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Authors: | Byung Chull An Seung Sik Lee Eun Mi Lee Jae Taek Lee Seung Gon Wi Hyun Suk Jung Woojun Park Sang Yeol Lee Byung Yeoup Chung |
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Institution: | (1) Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 1266 Sinjeong-dong, Jeongeup, Jeollabuk-do, 580-185, South Korea;(2) Bio-Energy Research Institute, Chonnam National University, 77 Yongbong-ro, Buk-gu, Gwangju, 500-757, South Korea;(3) Division of Electron Microscopic Research, Korea Basic Science Institute, Eoeun-dong, Daejeon, 305-333, South Korea;(4) Division of Environmental Sciences and Ecological Engineering, Korea University, Anam dong, Seongbuk-Gu, Seoul, 136-701, South Korea;(5) Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju, 660-701, South Korea; |
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Abstract: | Many proteins have been isolated from eukaryotes as redox-sensitive proteins, but whether these proteins are present in prokaryotes
is not clear. Redox-sensitive proteins contain disulfide bonds, and their enzymatic activity is modulated by redox in vivo.
In the present study, we used thiol affinity purification and mass spectrometry to isolate and identify 19 disulfide-bond-containing
proteins in Pseudomonas putida exposed to potential oxidative damages. Among these proteins, we found that a typical 2-Cys Prx-like protein (designated
PpPrx) displays diversity in structure and apparent molecular weight (MW) and can act as both a peroxidase and a molecular
chaperone. We also identified a regulatory factor involved in this structural and functional switching. Exposure of pseudomonads
to hydrogen peroxide (H2O2) caused the protein structures of PpPrx to convert from high MW complexes to low MW forms, triggering a chaperone-to-peroxidase
functional switch. This structural switching was primarily guided by the thioredoxin system. Thus, the peroxidase efficiency
of PpPrx is clearly associated with its ability to form distinct protein structures in response to stress. |
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Keywords: | Peroxiredoxin Molecular chaperone Peroxidase Functional switch Pseudomonas putida |
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