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Uncovering the in vivo function of the Hsp90 homolog in Escherichia coli

Wednesday, November 06, 2013 — Poster Session I

4:00 p.m. – 6:00 p.m.

FAES Academic Center (Upper-Level Terrace)




  • M Markovski
  • O Genest
  • JR Hoskins
  • S Wickner


Conserved from bacteria to humans, heat shock proteins (Hsps) are ubiquitous molecular chaperones that assist in protein folding during stress conditions. In particular, the members of the Hsp90 chaperone family are ATP-dependent molecular machines that refold non-native or unfolded proteins into their native conformations. In eukaryotes, Hsp90 is an essential protein and is required to remodel and activate hundreds of clients. During tumor progression, cancer cells exploit Hsp90 because it is needed for the function of tumor-promoting factors. In Escherichia coli, however, the activity of its Hsp90 homolog (Hsp90Ec) has remained elusive. Little is known about its function, and very few client proteins have been identified. The goal of this project is to identify and characterize the in vivo function of Hsp90Ec through genetic and cell biological methods. Our work will further our understanding of bacterial biology. Also, due to its high sequence similarity to eukaryotic Hsp90, characterizing the role(s) of Hsp90Ec will provide us with a better understanding of the functions of the Hsp90 family as a whole and provide new insight to develop better Hsp90 inhibitors for cancer treatment.

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