Heat shock protection against cold stress of Drosophila melanogaster.

Abstract

Heat shock protein synthesis can be induced during recovery from cold treatment of Drosophila melanogaster larvae. Survival of larvae after a cold treatment is dramatically improved by a mild heat shock just before the cold shock. The conditions which induce tolerance to cold are similar to those which confer tolerance to heat.Heat shock proteins are a group of proteins which are universally expressed in response to heat, heavy metals, and a variety of chemical treatments (1, 5, 10, 11). The major heat shock proteins synthesized in bacteria, plants, and mammals show a high degree of sequence homology (1, 5). These proteins are also synthesized during some periods in normal development.Transient resistance to killing by heat stress has been observed to be induced in many organisms by an initial exposure to a sublethal heat treatment (2, 7, 11). We have shown that conditions which induce thermotolerance in Drosophila melanogaster also induce the synthesis of heat shock proteins (7), and this correlation has been repeated many times in a variety of systems (1,5). Because of this and the universality of the response, it has been suggested that heat shock proteins play a role in protecting cells from damage caused by these stresses. The precise function of the heat shock proteins as well their role in stress protection are still uncertain.We show here that heat shock proteins are synthesized during recovery from prolonged exposure to cold in the absence of heat shock and that a mild heat treatment of the same kind which protects against death from heat shock also prevents death from exposure to cold.Induction of heat shock proteins by cold treatment. Drosophila larvae recovering from cold treatments of more than 8 h at 0°C synthesized the same set of heat shock or stress proteins that are made in response to heat shock (7, 9, 12). Figure 1 shows the proteins synthesized in larval salivary glands during recovery from 14 h at 0°C. Salivary glands were dissected from cold-shocked larvae that had been allowed to recover for 0, 10, 20, 30, or 40 min at 25°C. The salivary glands were labeled for 30 min with ['5S] methionine, and the proteins were separated on sodium dodecyl sulfate-polyacrylamide gels as described previously (8). An untreated 25°C control is shown in Fig. 1, lane C, as is a typical heat shock pattern from animals heated to 37°C (lane H). Clearly, all the major heat shock proteins appeared in the 20-min sample. The strongest heat shock protein synthesis patterns were seen not during the 30 min immediately following the cold treatment, but rather when larvae were allowed to recover for 30 or 40 min before being labeled. This suggests that the induction of the heat shock proteins may be a response to the shift from 0 to 25°C rather than a response to the 0°C treatment itself. We are currently doing * Corresponding author.RNA blots to determine directly the levels of hsp70 mRNA present at 0°C and during the recovery at 25°C.Experiments designed to evaluate the effects of different durations of cold treatments ...

Protein synthesis rates in Drosophila associate with levels of the hsr-omega nuclear transcript

“…Consistent with this view is mounting evidence that protein synthesis is important for both heat tolerance (Stephanou et al 1983) and cold tolerance (Burton et al 1988;Misener et al 2001) and that variation in hsr-omega influences both heat tolerance (McKechnie et al 1998;Rako et al 2007) and cold tolerance (Collinge et al 2008). While there is little doubt about the importance of variation in the hsps, particularly hsp70, in influencing thermal tolerance variation (Krebs and Feder 1997;Bettencourt et al 1999;Sørensen et al 2003), variation in hsr-omega via its effects on protein synthesis and its shutdown may also be an Omega-c relative to cyck Fig.…”

“…In these studies the kinetics of protein synthesis that was assessed in ovarian tissues following a heat shock was associated with changes in the timing and extent of hsp production, with timing and extent of housekeeping protein shutdown, and with heat stress survival differences between the lines. While a few other studies have asked if protein synthesis relates to thermal tolerance (Dingley and MaynardSmith 1968;Burton et al 1988;Misener et al 2001), and considerable research has shown how hsps and their genes are up-regulated following thermal stress (Lis and Wu 1994;Yost et al 1990), little effort has been made to investigate the shutdown of general protein synthesis and how this impinges on hsp production and thermotolerance.…”

Changes in nuclear phenotypes following cold shock in Panstrongylus megistus (Burmeister)

“…Even so, more than 50% of the P. megistus nymphs at different developmental phases survive for at least one month after a short cold shock (Garcia et al 1999b). While cryoprotectants are unknown in these insects, it is hypothesized that heat shock proteins (hsp) confer a certain amount of protection to P. megistus against cold in a similar way to that reported for some other insect species (Chen et al 1987, Burton et al 1988, Komatsu et al 1996. Indeed, cold tolerance may be induced in P. megistus (Garcia et al 1999a).…”

Survival and Molting Incidence after Heat and Cold Shocks in Panstrongylus megistus Burmeister

“…Based on data for other insect species, it is hypothesized that hsp synthesis may also be engaged in a certain protection of P. megistus organism against protein abnormalities resulting from the cold shock, mainly when it did not extend for very long periods of time and affected fully nourished specimens (Chen et al 1987, Burton et al 1988, Komatsu et al 1996.…”