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

Anuradha Balasubramanian | Zendy; Monica Markovski | Zendy; Joel R. Hoskins | Zendy; Shan M. Doyle | Zendy; Sue Wickner | Zendy

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

Author(s) -

Anuradha Balasubramanian,

Monica Markovski,

Joel R. Hoskins,

Shan M. Doyle,

Sue Wickner

Publication year - 2019

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.1904014116

Subject(s) - ftsz , tubulin , cell division , chaperone (clinical) , biology , filamentation , microbiology and biotechnology , hsp90 , heat shock protein , cytoskeleton , escherichia coli , mutant , biochemistry , microtubule , cell , gene , medicine , laser , physics , pathology , optics

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.

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