| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
184-385 |
DRI_Outcome |
denotes |
Previously, we demonstrated that species of the Stratiomyidae family exhibit higher tolerance to thermal stress in comparison with that of many representatives of Diptera, including Drosophila species. |
| T2 |
386-599 |
DRI_Challenge |
denotes |
We hypothesized that species of this group inherited the specific structures of their chaperones from an ancestor of the Stratiomyidae family, and this enabled the descendants to colonize various extreme habitats. |
| T3 |
600-703 |
DRI_Outcome |
denotes |
To explore this possibility, we cloned and expressed in Escherichia coli copies of the Hsp70 genes from |
| T4 |
726-803 |
DRI_Outcome |
denotes |
, a typical eurythermal species, and Drosophila melanogaster, for comparison. |
| T5 |
804-980 |
DRI_Background |
denotes |
To investigate the thermal sensitivity of the chaperone function of the inducible 70-kDa heat shock proteins from these species, we used an in vitro refolding luciferase assay. |
| T6 |
981-1166 |
DRI_Outcome |
denotes |
We demonstrated that under conditions of elevated temperature, S. singularior Hsp70 exhibited higher reactivation activity in comparison with D. melanogaster Hsp70 and even human Hsp70. |
| T7 |
1167-1344 |
DRI_Outcome |
denotes |
Similarly, S. singularior Hsp70 was significantly more thermostable and showed in vitro refolding activity after preheatment at higher temperatures than D. melanogaster paralog. |
| T8 |
1345-1666 |
DRI_Approach |
denotes |
Thermally induced unfolding experiments using differential scanning calorimetry indicated that Hsp70 from both Diptera species is formed by two domains with different thermal stabilities and that the ATP-binding domain of S. singularior is stable at temperatures 4 degrees higher than that of the D. melanogaster paralog. |
| T9 |
1667-1962 |
DRI_Outcome |
denotes |
To the best of our knowledge, this study represents the first report that provides direct experimental data indicating that the evolutionary history of a species may result in adaptive changes in the structures of chaperones to enable them to elicit protective functions at extreme environments. |
