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Background  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.    Results   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.    Conclusion  Modification of  Hsp70  copy number quantitatively and qualitatively affects the expression of multiple other stress-response genes. A positive association between absolute expression levels of  Hsp70  and other  Hsps  after thermal pretreatment suggests novel regulatory mechanisms. Severe heat shocks induce both novel gene expression patterns and almost total mortality in the  Hsp70  null strain: alteration of gene expression in this strain does not compensate for  Hsp70  loss but suggests candidates for overexpression studies.

bmc biology

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 Hsp70null flies