Pj. Diiorio et al., QUANTITATIVE EVIDENCE THAT BOTH HSC70 AND HSP70 CONTRIBUTE TO THERMALADAPTATION IN HYBRIDS OF THE LIVEBEARING FISHES POECILIOPSIS, Cell stress & chaperones, 1(2), 1996, pp. 139-147
The 70-kilodalton heat shock protein family is composed of both enviro
nmentally inducible (Hsp) and constitutively expressed (Hsc) family me
mbers. While the role of the constitutively expressed stress proteins
in thermotolerance is largely unknown, de novo expression of stress pr
oteins in response to elevated temperatures has been associated with i
ncreased thermotolerance in many cell lines, developing embryos and ad
ult organisms. Distinct, hemiclonal hybrids between the livebearing fi
sh species Poeciliopsis monacha and P. lucida varied in their abilitie
s to survive temperature stress, with survival being greatest when rat
es of temperature increase to 40 degrees C were slowest and when P. mo
nacha genomes were combined with a sympatric P. lucida genome. Quantif
ication of Hsp70 under heat shock conditions and Hsc70 under normal ph
ysiological conditions indicated that variation in survival among hemi
clones was best explained by the combined effects of these two protein
s. Similar complex interactions between maternal and paternal genomes
and rate of temperature increase were found to underlie patterns of su
rvival, Hsp70 accumulation and Hsc70 abundance. These data suggest tha
t the relationship between Hsps and thermotolerance is more intricate
than previously thought and that Hsps contribute to thermal adaptation
in these fishes through genetic interactions specific to particular e
nvironments.