Analytical assays of human HSP27 and thermal-stress survival of Escherichia coli cells that overexpress it.
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.
Takeuchi
Satoru
S
Department of Protein Research, ProstaColon, 85 NE, Takamatsu, Kahoku, Ishikawa 929-1215, Japan. takeuchi@coffee.ocn.ne.jp
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000032:analysis* / Q000096:biosynthesis*; D006358:Hot Temperature; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000032:analysis* / Q000096:biosynthesis*; D011994:Recombinant Proteins / Q000032:analysis / Q000096:biosynthesis; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D011994:Recombinant Proteins