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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe

  • Kim, Ji-Sun (Departments of Food and Nutrition, Chonnam National University) ;
  • Bang, Mi-Ae (Departments of Food and Nutrition, Chonnam National University) ;
  • Lee, Song-Mi (School of Biological Sciences and Technology, Chonnam National University) ;
  • Chae, Ho-Zoon (School of Biological Sciences and Technology, Chonnam National University) ;
  • Kim, Kang-Hwa (Departments of Food and Nutrition, Chonnam National University)
  • Published : 2010.03.31
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Abstract

Chaperone;Glutathione peroxidase;Peroxiredoxin;Schizosaccharomyces pombe;Thioredoxin peroxidase;To investigate the differences in the functional roles of peroxiredoxins (Prxs) and glutathione peroxidase (GPx) of Schizosaccharomyces pombe, we examined the peroxidase and molecular chaperone properties of the recombinant proteins. TPx (thioredoxin peroxidase) exhibited a capacity for peroxide reduction with the thioredoxin system. GPx also showed thioreoxin-dependent peroxidase activity rather than GPx activity. The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx. However, peroxidase activity was not observed for PMP20 (peroxisomal membrane protein 20). TPx, PMP20, and GPx inhibited thermal aggregation of citrate synthase at 43$^{\circ}C$, but BCP failed to inhibit the aggregation. The chaperone activities of PMP20 and GPx were weaker than that of TPx. The peroxidase and chaperone properties of TPx, BCP, and GPx of the fission yeast are similar to those of Saccharomyces cerevisiae. The fission yeast PMP20 without thioredoxin-dependent peroxidase activity may act as a molecular chaperone.

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References

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