Analytical assays of human HSP27 and thermal-stress survival of Escherichia coli cells that overexpress it

被引：16

作者：

Takeuchi, S ^{[1
]}

机构：

[1] ProstaColon, Dept Prot Res, Kahoku, Ishikawa 9291215, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 341卷 / 04期

关键词：

HSP27; chaperone-like activity; hydropathy; thermotolerance;

D O I：

10.1016/j.bbrc.2006.01.090

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

HSP27 is a small heat-shock protein (sHSP). Such proteins are produced in all organisms. These small HSPs exhibit chaperone-like activity that can bind to unfolded polypeptides and prevent uncontrolled protein aggregation in vitro. Cellular anti-apoptosis function and enhanced cell survival are correlated with increased expression of HSPs. This study presents a thermal-stress survival model for cells using the Escherichia coli expression system for which human HSP27, a recombinant protein, is inducible. Results show that E coli cells overexpressing human HSP27 have enhanced tolerance to 50 degrees C thermal stress. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：1252 / 1256

页数：5

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