• Korean Journal of Microbiology
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• v.52 no.4
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• pp.398-405
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• 2016

The Schizosaccharomyces pombe structural gene encoding bacterioferritin comigratory protein (BCP) was previously cloned using the shuttle vector pRS316 to generate the BCP-overexpressing plasmid pBCP10. The present work aimed to evaluate the thermoresistant properties of BCP against high temperature stress using the plasmid pBCP10. When the S. pombe cells were grown to the early exponential phase and shifted from $30^{\circ}C$ to $37^{\circ}C$ or $42^{\circ}C$, the S. pombe cells harboring pBCP10 grew significantly more at both $37^{\circ}C$ and $42^{\circ}C$ than the vector control cells. After 6 h of the shifting to higher incubation temperatures, they contained the lower reactive oxygen species (ROS) and nitrite content, an index of nitric oxide (NO), than the vector control cells. After the temperature shifts, total glutathione (GSH) content and total superoxide dismutase (SOD) activities were much higher in the S. pombe cells harboring pBCP10 than in the corresponding vector control cells. Taken together, the S. pombe BCP plays a thermoresistant role which might be based upon its ability both to down-regulate ROS and NO levels and to up-regulate antioxidant components, such as total GSH and SOD, and subsequently to maintain thermal stability.

• BMB Reports
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• v.43 no.3
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• pp.170-175
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• 2010

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.