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Abstract

All plants synthesize multiple families of small heat shock proteins (sHSP). A cDNA clone, Oshsp18.0-CII, encoding an 18.0 kDa class II sHSP was isolated from rice previously. The function of the rice class II sHSP was studied by overproduction of the Oshsp18.0-CII fusion protein in transformed Escherichia coli cells. The results suggest that heterologous expression of the Oshsp18.0-CII fusion protein increases thermotolerance of E. coli cells in vivo and provided thermoprotection to E. coli soluble proteins in vitro. The survival rate of Oshsp 18.0-CII fusion protein-accumulating cells treated at 50 degrees C for 1 h was almost 1000-fold higher than that of the control cells transformed with pET32a expression vector. Overproduction of the Oshsp18.0-CII fusion protein in E. coli also confers tolerance of E. coli cells to ultraviolet (UV) irradiation. The post-UV survival of the Oshsp18.0-CII fusion protein-accumulating cells is about 7.29-fold over that of the control cells transformed with pET32a expression vector when exposed to 1700 mu J of UV. There is almost no post-UV survival (<= 0.4%) in the untransformed cells after exposing to 900 mu J UV light.

Authors

Chang, Pi-Fang Linda;  Huang, Wen-Kuan;  Lin, Ying-Hong;  Chen, Yuhsin;  Chang, Tao-Ho

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