Document Type
Article
Publication Date
2-2001
Publication Title
Biochemical Genetics
Disciplines
Biology
Abstract
Acclimation to environmental change can impose costs to organisms. One potential cost is the change in cell metabolism that follows a physiological response, e.g., high expression of heat shock proteins may alter specific activity of important enzymes. We examined the significance of this cost in a pair of Drosophila melanogaster lines transformed with additional copies of a gene that encodes the heat shock protein, Hsp70. Heat shock induces Hsp70 expression in all lines, but lines with extra copies produce much more Hsp70 than do excision control strains. The consequence of this supranormal Hsp70 expression is to reduce specific activity of both enzymes analyzed, adult alcohol dehydrogenase (ADH), which is heat sensitive, and lactate dehydrogenase, which is not. Strain differences were most pronounced under those conditions where Hsp70 expression was maximized, and not where the heat stress denatured proteins. That result supported the idea that Hsp70 expression is constrained evolutionarily by its tendency to bind nascent peptides when overabundant within the cell.
DOI
10.1023/A:1002701420091
Version
Postprint
Publisher's Statement
The final publication is available at Springer via http://dx.doi.org/10.1023/A:1002701420091
Recommended Citation
Krebs R and Holbrook S. 2001. Reduced enzyme activity following Hsp70 overexpression in drosophila melanogaster. Biochem Genet 39(1-2):73-82.
Volume
39
Issue
1-2
