Department Chair

Gregory J. Wadsworth Ph.D., Chair and Associate Professor of Biology

Date of Award


Access Control

Campus-Only Access

Degree Name

Biology, M.A.


Biology Department


Douglas P. Easton, Ph.D., Professor of Biology

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First Reader

Douglas P. Easton, Ph.D., Professor of Biology

Second Reader

Gregory J. Wadsworth, Ph.D., Chair and Associate Professor of Biology

Third Reader

I. Martha. Skerrett, Ph.D., Associate Professor of Biology


Heat shock proteins (hsps) are a group of highly conserved proteins that are well distributed in phylogeny. Drosophila melanogaster embryos are endowed with large amounts of hsp110 synthesized in the ovaries of female flies and its expression level remains constant throughout the embryogenesis which indicates the necessity for hsp110. It has been found that hsp70, hsp90 and hsp110 act as molecular chaperones that assist in protein folding and degradation of aggregated proteins. Association between hsp70 and hsp110, hsp90 and hsp110, as co-chaperone complexes have been observed in mammalian cells, but these observations have not yet been established in Drosophila.

In the current study, co-immunoprecipitation with Nano Trap® beads was used to determine the association between hsp110, hsp70 and hsp90. We find that hsp110 form a complex with hsp90 in all life stages of Drosophila, however this hsp110-hsp90 complex is disrupted under heat shock conditions. This clearly shows that the chaperone cycle between these two proteins is heat dependent.

The hypothesized hsp110-hsp70-hsp90 or hsp110-hsp70 complex has not been seen in this study which is different from the mammalian and yeast system. Further experiments using different approaches to the isolation of the complexes are needed to reexamine the complexes for analysis of their composition to confirm that the hsp70-hsp110 chaperone cycle occurs in Drosophila. These findings of the chaperone machinery would provide a better understanding of the function of hsp110, that whether hsp110 serves as a chaperone by itself or as a co-chaperone with other associated proteins in Drosophila.

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