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Co-expression of this protein with the disease protein not only fails to suppress, but actually enhances, degeneration. This finding suggests that toxicity to the polyglutamine protein is sensitive to the levels of the Hsp70 family of molecular chaperones, with added Hsp70 preventing degeneration, whereas interference with endogenous chaperone activity promotes degeneration. We also investigated the role of the Hsp70 co-chaperone Hsp40 in protein pathogenicity, by creating transgenic flies that overexpress the fly counterpart of the human Hdj1 class of molecular chaperone, dHdj1.

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