Thermodynamics of heat-shock response.
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 temperature T0 approximately 23 degrees C, thereby mimicking the nonmonotonous stability of proteins at low temperature. This suggests that stability related to hot as well as cold unfolding of proteins is directly implemented in the biological control of protein folding.
Bourke Arnvig
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Institute of Molecular Biology, Oster Farimagsgade 2A, 1353 Copenhagen K, Denmark.
Pedersen
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Sneppen
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D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics*; D006358:Hot Temperature; D007700:Kinetics; D008954:Models, Biological; D018832:Molecular Chaperones / Q000235:genetics*; D013816:Thermodynamics
D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; C063842:dnaK protein, E coli