RESUMO
Thermotolerance was studied in a wide spectrum of Drosophila species and strains originating from different climatic zones and considerably differing from one another in the ambient temperature of their habitats. The species that lived in hot climate have a higher thermotolerance. Most species of the virilis group exhibited positive correlation between the HSP70 accumulation after heat exposure and thermotolerance; however, this correlation was absent in some species and strains. For example, the D. melanogaster Oregon R strain, which had the highest sensitivity to heat shock (HS) among all strains and species studied, displayed the maximum level of HSP70 proteins after HS. The patterns of induction of various heat shock protein (HSP) families after heat exposure in a wide spectrum of Drosophila species were compared. The results obtained suggest that the HSP40 and low-molecular-weight HSPs (lmwHSPs) play a significant role in thermotolerance and adaptation to hot climate. Polymorphism in hsp70 gene clusters of Drosophila and variation in the numbers of gene copies and hsp70 isoforms in group virilis were found. The evolutionary role of the variation in the number of hsp70 gene copies observed in the strains and species of genus Drosophila is discussed.
Assuntos
Evolução Biológica , Proteínas de Drosophila/genética , Drosophila/fisiologia , Resposta ao Choque Térmico/genética , Animais , Proteínas de Drosophila/metabolismo , Dosagem de Genes , Variação Genética , Proteínas de Choque Térmico HSP40 , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Família Multigênica , Especificidade da EspécieRESUMO
Drosophila melanogaster collected in sub-equatorial Africa in the 1970s are remarkably tolerant of sustained laboratory culture above 30 degrees 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.
Assuntos
Drosophila melanogaster/genética , Drosophila melanogaster/fisiologia , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/fisiologia , Aclimatação , África Subsaariana , Animais , Sequência de Bases , Primers do DNA/genética , Genes de Insetos , Temperatura Alta , Cinética , Família Multigênica , Fenótipo , Polimorfismo Genético , RNA Mensageiro/genética , RNA Mensageiro/metabolismoRESUMO
Here we studied the response to heat shock in a desert D. melanogaster strain TT capable of living and propagating at 32 degrees C and the standard Oregon R strain. The TT strain proved to be more resistant to extreme temperatures. On the other hand, the observed high thermotolerance of the strain was not accompanied by a higher level of HSP70 synthesis. Conversely, reliably smaller amounts of HSP70 were synthesized in the TT strain as compared to Oregon R under all shock temperatures except the critical one (39.5 degrees C). Differences in both the structure of HSP70 genes and the pattern of all heat shock proteins have been observed between the studied strains. The role of the heat shock system in the adaptation to hyperthermia is discussed.
Assuntos
Proteínas de Drosophila/biossíntese , Drosophila melanogaster/metabolismo , Proteínas de Choque Térmico HSP70/biossíntese , Resposta ao Choque Térmico/fisiologia , Animais , Proteínas de Drosophila/genética , Drosophila melanogaster/genética , Eletroforese em Gel Bidimensional , Proteínas de Choque Térmico HSP70/genética , RNA Mensageiro/análise , RNA Mensageiro/metabolismoRESUMO
We compare the properties and activation of heat-shock transcription factor (HSF1) and the synthesis of a major family of heat-shock proteins (HSP70) in lizard species inhabiting ecological niches with strikingly different thermal parameters. Under normal non-heat-shock conditions, all desert-dwelling lizard species studied so far differ from a northern, non-desert species (Lacerta vivipara) in the electrophoretic mobility and content of proteins constitutively bound to the regulatory heat-shock elements in the heat-shock gene promoter. Under these conditions, levels of activated HSF1 and of both HSP70 mRNA and protein are higher in the desert species than in the non-desert species. Upon heat shock, HSF1 aggregates in all species studied, although in desert species HSF1 subsequently disaggregates more rapidly. Cells of the northern species have a lower thermal threshold for HSP expression than those of the desert species, which correlates with the relatively low constitutive level of HSPs and high basal content of HSF1 in their cells.
