| Literature DB >> 16466698 |
Abstract
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.Entities:
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Year: 2006 PMID: 16466698 DOI: 10.1016/j.bbrc.2006.01.090
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575