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doi:10.1534/genetics.105.048793
A more recent version of this article appeared on January 1, 2006.
REGULAR RESEARCH PAPERS |
Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock, and neurodegeneration
Wei J Gong 1 and Kent G Golic 2*
1 Stowers Institute
2 University of Utah
* To whom correspondence should be addressed. E-mail: golic{at}biology.utah.edu.
Submitted on July 26, 2005
Revised on September 2, 2005
Accepted on 21 September 2005
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.
Key Words: Drosophila, Hsp70, chaperone, temperature-sensitive, thermotolerance
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