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嗜热古菌 Sulfolobus solfataricus P2 的小分子热休克蛋白 HSP20 的热耐受性和分子伴侣功能。

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

机构信息

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

出版信息

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

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 thermo-denatured citrate synthase and insulin B chain. These results suggest that S.so-HSP20 promotes thermotolerance and engages in chaperone-like activity during the stress response.

摘要

小热休克蛋白存在于所有三个域(古细菌、细菌和真核生物)中,具有分子伴侣活性,通过与未折叠的多肽结合,防止体外蛋白质聚集。来自嗜热古细菌 Sulfolobus solfataricus P2 的小热休克蛋白(S.so-HSP20)的功能尚未描述。在本研究中,我们使用实时聚合酶链反应分析测量了 S. solfataricus P2 中 S.so-HSP20 的 mRNA 表达,发现它受温度诱导,温度明显低于(60°C)或高于(80°C)S. solfataricus P2 的最适温度(75°C)。S.so-HSP20 mRNA 的表达也受到冷休克(4°C)的上调。表达 S.so-HSP20 的大肠杆菌细胞对温度冲击(50°C、4°C)表现出更高的耐热性。通过测定酶活性,发现 S.so-HSP20 可促进热变性柠檬酸合酶和胰岛素 B 链的正确折叠。这些结果表明,S.so-HSP20 在应激反应中促进耐热性并发挥伴侣样活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/43a3/3227843/2993edca7169/12192_2011_289_Fig1_HTML.jpg

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