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Functional switching of a novel prokaryotic 2-Cys peroxiredoxin (PpPrx) under oxidative stress

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Cell Stress and Chaperones Aims and scope

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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Acknowledgments

This project was carried out under the Nuclear R&D Program of the Ministry of Science and Technology (http://WWW.mest.go.kr), Republic of Korea. EM work was supported by KBSI grant T3021A to Jung, HS.

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Authors and Affiliations

  1. Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 1266 Sinjeong-dong, Jeongeup, Jeollabuk-do, 580-185, South Korea

    Byung Chull An, Seung Sik Lee, Eun Mi Lee, Jae Taek Lee & Byung Yeoup Chung

  2. Bio-Energy Research Institute, Chonnam National University, 77 Yongbong-ro, Buk-gu, Gwangju, 500-757, South Korea

    Seung Gon Wi

  3. Division of Electron Microscopic Research, Korea Basic Science Institute, Eoeun-dong, Daejeon, 305-333, South Korea

    Hyun Suk Jung

  4. Division of Environmental Sciences and Ecological Engineering, Korea University, Anam dong, Seongbuk-Gu, Seoul, 136-701, South Korea

    Woojun Park

  5. Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju, 660-701, South Korea

    Sang Yeol Lee

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  1. Byung Chull An
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  2. Seung Sik Lee
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Correspondence to Byung Yeoup Chung.

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Supplementary Fig. 1

A Each SEC fraction was separated by 10% native-PAGE. B Each SEC fraction was separated by 12% non-reducing-PAGE. PpPrx recombinant protein was stained with Coomassie Brilliant Blue R-250. F-1 lane F-1 fraction of PpPrx, F-2 lane F-2 fraction of PpPrx (GIF 61 kb)

High-resolution image (TIFF 735 kb)

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An, B.C., Lee, S.S., Lee, E.M. et al. Functional switching of a novel prokaryotic 2-Cys peroxiredoxin (PpPrx) under oxidative stress. Cell Stress and Chaperones 16, 317–328 (2011). https://doi.org/10.1007/s12192-010-0243-5

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  • DOI: https://doi.org/10.1007/s12192-010-0243-5

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