title: Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert.
abstract: The ant Cataglyphis lives in the Sahara desert and is one of the most thermotolerant land animals known. It forages at body temperatures above 50 degrees C, and the critical thermal maxima are at 53.6 +/- 0.8 degrees C for Cataglyphis bombycina and 55.1 +/- 1.1 degrees C for Cataglyphis bicolor. The synthesis and accumulation of heat shock proteins (HSPs) were analyzed in Cataglyphis and compared to Formica, an ant living in more moderate climates, and to two Drosophila species. In Cataglyphis, protein synthesis continues at temperatures up to 45 degrees C as compared to 39 degrees C for Formica and Drosophila. The two Drosophila species, Drosophila melanogaster and Drosophila ambigua, differ with respect to their maximal induction of HSP synthesis and accumulation by 3-4 degrees C. In contrast, the two ant species accumulate HSPs prior to their exposure to heat, and in Cataglyphis the temperature of maximal HSP induction by de novo protein synthesis is only 2 degrees C higher than in Formica. These findings are interpreted as preadaption of the ants prior to exposure to high temperatures.
authors.affiliation: Biozentrum, University of Basel, Switzerland.
authors.forename: W J
authors.initials: WJ
authors.lastname: Gehring
authors.forename: R
authors.initials: R
authors.lastname: Wehner
mesh_terms: D000064:Acclimatization; D000818:Animals; D001000:Ants / Q000378:metabolism / Q000502:physiology*; D015153:Blotting, Western; D003080:Cold Temperature; D003889:Desert Climate; D004330:Drosophila / Q000378:metabolism; D004331:Drosophila melanogaster / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D006358:Hot Temperature; D008715:Methionine / Q000378:metabolism; D013045:Species Specificity; D013462:Sulfur Radioisotopes
chemical_list: D006360:Heat-Shock Proteins; D013462:Sulfur Radioisotopes; D008715:Methionine