Title:

Effects of Acetylation on the Conformation of Hsp90 in Embryonic Stem Cells

A crucial protein for the survival of eukaryotic cells is the highly conserved molecular chaperone, heat-shock protein 90 (Hsp90). Due to its conformational flexibility, Hsp90 interacts with many cochaperones throughout its ATPase cycle, regulating over 200 client proteins. This is a function of Hsp90 that becomes exploited in cells under stressed conditions to buffer cytotoxic effects, promote homeostasis of the proteome and enhance cell survival. For instance, the expression of chaperone proteins in tumors is nearly 2-3 times that of levels in non-tumorigenic tissue. Additionally, in half of all tumor cells, Hsp90 has been shown to exist in a large multi-chaperone complex referred to as the epichaperome. Post-translational modifications (PTM’s) potentially may serve as a mechanism that regulate its function within the epichaperome. One such PTM is acetylation on lysine residues, where two novel sites have been identified on Hsp90 from mouse embryonic stem cells (mESCs) and we seek to further elucidate the importance of these acetyl sites and their regulation of the chaperone.

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