English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Hsp90 is a molecular chaperone that participates in protein remodeling and activation. We previously demonstrated that Hsp90 causes cell filamentation when highly expressed inE. coli . Here we show that cells filament due to overexpression of Hsp90Ec because FtsZ, a bacterial tubulin homolog essential for cell division, fails to assemble into FtsZ rings. In vitro, Hsp90Ec interacts with FtsZ and inhibits FtsZ polymerization. Moreover,E. coli deleted for the Hsp90Ec gene,htpG , turn over FtsZ more rapidly than wild-type cells, and the length of ΔhtpG cells is reduced compared to wild-type cells. Altogether, these results suggest that Hsp90Ec is a modulator of cell division, and imply that the polypeptide-holding function of Hsp90 may be a biologically important chaperone activity.

Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog