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Cell Stress Chaperones. 2012 Jan;17(1):103-8. doi: 10.1007/s12192-011-0289-z. Epub 2011 Aug 20.

Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2.

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College of Life Sciences, Zhejiang University and Key Laboratory of Conservation Biology for Endangered Wildlife of the Ministry of Education, Hangzhou 310058, China.


Small heat shock proteins are ubiquitous in all three domains (Archaea, Bacteria and Eukarya) and possess molecular chaperone activity by binding to unfolded polypeptides and preventing aggregation of proteins in vitro. The functions of a small heat shock protein ( from the hyperthermophilic archaeon, Sulfolobus solfataricus P2 have not been described. In the present study, we used real-time polymerase chain reaction analysis to measure mRNA expression of in S. solfataricus P2 and found that it was induced by temperatures that were substantially lower (60°C) or higher (80°C) than the optimal temperature for S. solfataricus P2 (75°C). The expression of mRNA was also up-regulated by cold shock (4°C). Escherichia coli cells expressing showed greater thermotolerance in response to temperature shock (50°C, 4°C). By assaying enzyme activities, was found to promote the proper folding of thermo-denatured citrate synthase and insulin B chain. These results suggest that promotes thermotolerance and engages in chaperone-like activity during the stress response.

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