Abstract
It is a common statement that heat-shock impairs cellular functions because some essential proteins are heat-denaturated. This statement relies mostly on indirect arguments developped by several workers (Hightower, 1980). The fate of such denatured proteins is matter for discussion: are they degraded or renatured? A priming non-lethal heat-shock stimulates transiently the synthesis of the heat-shock proteins (HSP) and increases transiently the cell resistance against a second challenging stress (Subjeck and Sciandra, 1982). Is this thermotolerant state due to a protective effect against thermal denaturation or to a better repair of the damaged proteins? What is the behaviour of the heat-shock proteins?
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© 1991 Springer-Verlag Berlin Heidelberg
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Bensaude, O., Dubois, MF., Legagneux, V., Nguyen, V.T., Pinto, M., Morange, M. (1991). Early Effects of Heat Shock on Enzymes: Heat Denaturation of Reporter Proteins and Activation of a Protein Kinase which Phosphorylates the C-terminal Domain of RNA Polymerase II. In: Maresca, B., Lindquist, S. (eds) Heat Shock. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76679-4_10
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DOI: https://doi.org/10.1007/978-3-642-76679-4_10
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