Abstract
Acquired thermotolerance, measured either as increased cell viability following a lethal heat shock or by translational thermotolerance, appears rapidly following a 'priming' heat treatment, but also decays rapidly. 4 hours after priming heating thermotolerance is reduced by > 50% and by 9 hours it is virtually undetectable. Heat-shock protein 70 (Hsp70) turns over with a half-life of approximately 2 hours, and the decline in its intracellular abundance parallels the loss of acquired thermotolerance. Continuous heat shock extends the half-life of Hsp70 to approximately 7 hours. When Hsp70 is expressed at normal temperature using a metallothionein promoter, only partial acquired translational thermotolerance results. The results suggest that acquired thermotolerance is tightly regulated in Drosophila and partly, but not wholly, determined by post-translational regulation of Hsp70 levels.
