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The Journal of Experimental Biology 204, 1869-1881 (2001)
© 2001 The Company of Biologists Limited

A DROSOPHILA MELANOGASTER Strain From Sub-Equatorial Africa Has Exceptional Thermotolerance But Decreased Hsp70 Expression

Olga G. Zatsepina¹, Vera V. Velikodvorskaia¹, Vasilii B. Molodtsov¹, David Garbuz¹, Daniel N. Lerman², Brian R. Bettencourt³, Martin E. Feder^2,3,* and Michael B. Evgenev¹

¹ Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 117984 Moscow, Russia,
² The Committee on Evolutionary Biology and
³ Department of Organismal Biology and Anatomy, The University of Chicago, 1027 East 57th Street, Chicago, IL 60637, USA

*Author for correspondence (e-mail: m-feder{at}uchicago.edu)

Accepted March 19, 2001

Drosophila melanogaster collected in sub-equatorial Africa in the 1970s are remarkably tolerant of sustained laboratory culture above 30°C and of acute exposure to much warmer temperatures. Inducible thermotolerance of high temperatures, which in Drosophila melanogaster is due in part to the inducible molecular chaperone Hsp70, is only modest in this strain. Expression of Hsp70 protein and hsp70 mRNA is likewise reduced and has slower kinetics in this strain (T) than in a standard wild-type strain (Oregon R). These strains also differed in constitutive and heat-inducible levels of other molecular chaperones. The lower Hsp70 expression in the T strain apparently has no basis in the activation of the heat-shock transcription factor HSF, which is similar in T and Oregon R flies. Rather, the reduced expression may stem from insertion of two transposable elements, H.M.S. Beagle in the intergenic region of the 87A7 hsp70 gene cluster and Jockey in the hsp70Ba gene promoter. We hypothesize that the reduced Hsp70 expression in a Drosophila melanogaster strain living chronically at intermediate temperatures may represent an evolved suppression of the deleterious phenotypes of Hsp70.

Key words: Drosophila melanogaster, evolutionary physiology, heat-shock protein, Hsp70, molecular chaperone, transposable element

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