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摘要:
Small heat shock proteins (sHSPs) exist ubiquitously among all organisms, with a variety of functions. All small heat shock proteins assemble into a native large oligomeric state containing 9-40 monomers. The sHSPs show chaperone-like activity to prevent the aggregation of nonnative proteins under stressful cellular conditions such as non-optimal temperatures, pH changes, osmotic pressure, and exposure to toxic chemicals. It was found that a common dimeric subunit of sHSPs might be the major active species, but whether the native large oligomeric state is only a storage state or a state crucial to its molecular chaperone activity is still under debate. The native large oligomeric state of the small heat shock protein from a hyperthermophilic methanarchaeon, Methanococcus jannaschii (Mj HSP 16.5), is a stable icositetramer, which is a symmetric hollow sphere that is very stable even at 85℃, and no small active subunit has been detected till now. Our results show that Mj sHSP 16.5 changes into small and active oligomeric state at pH 3, likely as octamers (average result) at 25℃, and dimers at 65℃. The dimer of Mj HSP 16.5 at pH 3.0 and 65℃ is very active and efficient, even 7-fold more efficient than the high-temperature-activated icositetramer at neutral pH. Monomer exchange can be observed between dimers of Mj HSP 16.5 at pH 3.0 and 65℃. These results not only demonstrate that the icositetramer structure of Mj sHSP16.5 is not necessary for its molecular chaperone activity, but also suggest that Mj sHSP16.5 is a very efficient chaperone acting at high temperature and under the acidic condition. Even though it is not clear whether the native environment of Methanococcus jannaschii is acidic or not, given its ability to excrete acidic compounds, it is likely that Methanococcus jannaschii will encounter acidic internal or external environments at high temperature. Our results demonstrate that Mj HSP 16.5 may help Methanococcus jannaschii to survive better under those extreme environmental conditions.
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篇名 High activity of Mj HSP16.5 under acidic condition
来源期刊 中国科学B辑(英文版) 学科
关键词
年,卷(期) 2009,(3) 所属期刊栏目
研究方向 页码范围 325-331
页数 7页 分类号
字数 语种 英文
DOI 10.1007/s11426-008-0158-5
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期刊影响力
中国科学:化学(英文版)
月刊
1674-7291
11-5839/O6
16开
北京东黄城根北街16号
1950
eng
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4060
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0
总被引数(次)
11421
相关基金
国家自然科学基金
英文译名:the National Natural Science Foundation of China
官方网址:http://www.nsfc.gov.cn/
项目类型:青年科学基金项目(面上项目)
学科类型:数理科学
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