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Mechanism of Stress-dependent Structural Change of Yeast Prx  

Kang, Ji-Seoun (Devision of Electron Microscopy, Korea Basic Science Institute)
Cheong, Gang-Won (Division of Applied Life Science, Gyeongsang National University, Environmental Biotechnology National Core Research Center)
Publication Information
Applied Microscopy / v.35, no.4, 2005 , pp. 16-23 More about this Journal
Abstract
Peroxiredoxins (Prxs) are a superfamily of thiol-specific antioxidant proteins present in all organism and involved in the hydroperoxide detoxification of the cell. To determine the structural organization of yeast-Prx, electron microscopic analysis was performed. The average images of yeast-Prxs revealed three different structure, i.e. spherical-shaped structure, ring-shaped structure and irregularly-shaped small particles. In order to analyze the conformational change of yeast-Prx by reduction and oxidation, Prxs were subjected to DTT and $H_2O_2$. In presence of DTT, yeast-Prx showed a high tendency to form a decamer. However, they changed into dimeric or spherical structure in the oxidized state. Here we also show ionic interaction between dimeric subunits is primarily responsible for yeast-Prx oligomerization.
Keywords
Electron microscopy; Peroxiredoxins (Prxs); Thiol-specific antioxidant protein;
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