Heat shock proteins (Hsps) were first described by Tissières in 1974 in the salivary glands of Drosophila third instar larvae exposed to sub-lethal temperatures (temperature shift of 20–35 °C). Hsps were then discovered in all living organisms, from bacteria to human including plants (Lindquist and Craig 1988). Five families of heat shock proteins have been described: the HspH (large Hsps), 90 kDa (HspC-Hsp90), 70 kDa (HspA-Hsp70), 60 kDa (HspD-Hsp60), and the 20–30 kDa small heat shock proteins (HspB-small Hsps, sHsps). The interest in these proteins was stimulated by discovering that their expression can be triggered by many environmental stress conditions as well as by toxins known to alter the folding of proteins.This lead to the finding that Hsps are molecular chaperones whose function is to attenuate stress-induced damages in protein folding and...
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