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Originally published as Genetics Published Articles Ahead of Print on October 3, 2005.
Genetics, Vol. 172, 275-286, January 2006, Copyright © 2006
doi:10.1534/genetics.105.048793
Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration
Wei J. Gong1 and Kent G. Golic2
Department of Biology, University of Utah, Salt Lake City, Utah 84112
2 Corresponding author: Department of Biology, University of Utah, 257 South 1400 East, Room 201, Salt Lake City, UT 84112.
E-mail: golic{at}biology.utah.edu
The heat-shock response is a programmed change in gene expression carried out by cells in response to environmental stress, such as heat. This response is universal and is characterized by the synthesis of a small group of conserved protein chaperones. In Drosophila melanogaster the Hsp70 chaperone dominates the profile of protein synthesis during the heat-shock response. We recently generated precise deletion alleles of the Hsp70 genes of D. melanogaster and have used those alleles to characterize the phenotypes of Hsp70-deficient flies. Flies with Hsp70 deletions have reduced thermotolerance. We find that Hsp70 is essential to survive a severe heat shock, but is not required to survive a milder heat shock, indicating that a significant degree of thermotolerance remains in the absence of Hsp70. However, flies without Hsp70 have a lengthened heat-shock response and an extended developmental delay after a non-lethal heat shock, indicating Hsp70 has an important role in recovery from stress, even at lower temperatures. Lack of Hsp70 also confers enhanced sensitivity to a temperature-sensitive lethal mutation and to the neurodegenerative effects produced by expression of a human polyglutamine disease protein.
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