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The Escherichia coli Hsp90 homolog plays a role during bacterial cell division

Thursday, September 17, 2015 — Poster Session II

12:00 p.m. – 1:30 p.m.
FAES Terrace


  • M Markovski
  • 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 Hsp90 family of ATP-dependent molecular chaperones are abundantly expressed and highly conserved proteins needed for the folding, stability and function of various cellular factors. In eukaryotes, Hsp90 is essential and required to remodel and activate hundreds of clients required for cell survival. In pathogenic bacteria, the Hsp90 homolog is an important virulence factor required for bacterial growth in macrophages and acute infection. However, little is known about Escherichia coli Hsp90 (Hsp90Ec). While nonessential, Hsp90Ec is abundant under normal conditions, and its levels are further increased during stress conditions. Here, we investigate the role that Hsp90Ec plays in bacterial cells. Recently, our group showed that overexpression of Hsp90Ec causes cells to filament. There are several conditions that can cause cells to become filamentous, including a block in cell division. To determine whether inhibition of the essential complex required for cell division and constriction (the divisome) causes this filamentous phenotype, we visualized early divisome formation using fluorescence microscopy in cells overexpressing Hsp90Ec and observed very few divisome rings, suggesting that high levels of Hsp90Ec inhibit divisome formation (and thus cell division) early. Our work further suggests that Hsp90Ec may play a role during bacterial cell division by potentially regulating FtsZ, a tubulin homolog and the first essential divisome protein.

Category: Microbiology and Infectious Diseases