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

Dong-Chol Li, Fan Yang, Bo Lu, Dian-Fu Chen and Wei-Jun Yang
Cell Stress & Chaperones
Vol. 17, No. 1 (JANUARY 2012), pp. 103-108
Published by: Cell Stress Society International in partnership with Springer
Stable URL: http://www.jstor.org/stable/41412290
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2
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Abstract

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 (S. SO-HSP20) 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 S. SO-HSP20 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 S. so-HSP20 mRNA was also up-regulated by cold shock (4°C). Escherichia coli cells expressing S. SO-HSP20 showed greater thermotolerance in response to temperature shock (50°C, 4°C). By assaying enzyme activities, S. SO-HSP20 was found to promote the proper folding of thermodenatured citrate synthase and insulin chain. These results suggest that S. so-HSP20 promotes thermotolerance and engages in chaperone-like activity during the stress response.

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