Heat shock response
The cellular response to heat shock includes the transcriptional up-regulation of genes encoding heat shock proteins (HSPs) as part of the cell's internal repair mechanism. They are also called stress-proteins. and respond to heat, cold and oxygen deprivation by activating several cascade pathways. HSPs are also present in cells under perfectly normal conditions. Some HSPs, called chaperones, ensure that the cell’s proteins are in the right shape and in the right place at the right time. For example, HSPs help new or misfolded proteins to fold into their correct three-dimensional conformations, which is essential for their function. They also shuttle proteins from one compartment to another inside the cell, and target old or terminally misfolded proteins to proteases for degradation. Heat shock proteins are also believed to play a role in the presentation of pieces of proteins (or peptides) on the cell surface to help the immune system recognize diseased cells.
The up-regulation of HSPs during heat shock is generally controlled by a single transcription factor; in eukaryotes this regulation is performed by heat shock factor (HSF), while σ32 is the heat shock sigma factor in Escherichia coli.
Inducing heat shock
In fish that survive at 0 °C, heat shock can be induced with temperatures as low as 5 °C, whereas thermophilic bacteria that proliferate at 50 °C will not express heat shock proteins until temperatures reach approximately 60 °C. The process of heat shocking can be done in a CO2 incubator, O2 incubator, or a hot water bath.
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