Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster.

@article{Morrow2006DifferencesIT,
  title={Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster.},
  author={Genevi{\`e}ve Morrow and John J. Heikkila and Robert M Tanguay},
  journal={Cell stress & chaperones},
  year={2006},
  volume={11 1},
  pages={51-60}
}
The Drosophila melanogaster family of small heat shock proteins (sHsps) is composed of 4 main members (Hsp22, Hsp23, Hsp26, and Hsp27) that display distinct intracellular localization and specific developmental patterns of expression in the absence of stress. In an attempt to determine their function, we have examined whether these 4 proteins have chaperone-like activity using various chaperone assays. Heat-induced aggregation of citrate synthase was decreased from 100 to 17 arbitrary units in… CONTINUE READING
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