BACKGROUND Specialized cellular defense mechanisms prevent damage from chemical, biological, and physical hazards. The heat shock proteins have been recognized as key chaperones that maintain cell survival against a variety of exogenous and endogenous stress signals including noxious temperature. However, the role of heat shock proteins in nociception remains poorly understood. We carried out a...

sHSP (small heat-shock protein) IbpB (inclusion-body-binding protein B) from Escherichia coli is known as an ATP-independent holding chaperone which prevents the insolubilization of aggregation-prone proteins by forming stable complexes with them. It was found that the chaperone function of IbpB is greatly modulated by the ambient temperature, i.e. when the temperature increases from normal to ...

1. Introduction Molecular chaperones function in a range of protein homeostatic events, including cotranslational protein folding, assembly and disassembly of protein complexes, and protein transport across membranes. Many molecular chaperones are also known as heat-shock proteins, which refers to their regulation by stress conditions as diverse as infection with viral and bacterial agents, exp...

We have investigated the role of the double-stranded RNA-dependent protein kinase gene (pkr) in the regulation of the heat shock response. We show that the pkr gene is essential for efficient activation of the heat shock response and that pkr disruption profoundly inhibits heat shock protein 70 (HSP70) synthesis and blocks the development of thermotolerance. Despite these profound effects, pkr ...

Production of heat-shock proteins is induced when a living cell is exposed to a rise in temperature. The heat-shock response of protein DnaK synthesis in E.coli for temperature shifts T-->T+DeltaT and T-->T-DeltaT is measured as a function of the initial temperature T. We observe a reversed heat shock at low T. The magnitude of the shock increases when one increases the distance to the temperat...