Inducible and constitutive heat shock gene expression responds to modification of Hsp70 copy number in Drosophila melanogaster but does not compensate for loss of thermotolerance in Hsp70 null flies.

BMC Biology
Brian R BettencourtBrian W Drohan

Abstract

The heat shock protein Hsp70 promotes inducible thermotolerance in nearly every organism examined to date. Hsp70 interacts with a network of other stress-response proteins, and dissecting the relative roles of these interactions in causing thermotolerance remains difficult. Here we examine the effect of Hsp70 gene copy number modification on thermotolerance and the expression of multiple stress-response genes in Drosophila melanogaster, to determine which genes may represent mechanisms of stress tolerance independent of Hsp70. Hsp70 copy number in four strains is positively associated with Hsp70 expression and inducible thermotolerance of severe heat shock. When assayed at carefully chosen temperatures, Hsp70 null flies are almost entirely deficient in thermotolerance. In contrast to expectations, increasing Hsp70 expression levels induced by thermal pretreatment are associated with increasing levels of seven other inducible Hsps across strains. In addition, complete Hsp70 loss causes upregulation of the inducible Hsps and six constitutive stress-response genes following severe heat shocks. Modification of Hsp70 copy number quantitatively and qualitatively affects the expression of multiple other stress-response genes. A positi...Continue Reading

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Citations

Sep 18, 2010·BMC Evolutionary Biology·Kazuo H TakahashiSiu F Lee
Mar 21, 2013·BMC Evolutionary Biology·Luke A Hoekstra, Kristi L Montooth
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Methods Mentioned

BETA
dissection
genetic modification
PCR
electrophoresis
thermal treatments
transgenic
thermal
PCRs

Software Mentioned

Primer3
RAD MyIQ
BIO
SAS

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