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Large ring polymers align FtsZ polymers for normal septum formation

Lookup NU author(s): Erkam Gundogdu, Dr Yoshikazu Kawai, Dr Nada Pavlendova, Professor Jeff Errington, Dr Leendert Hamoen

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Abstract

Cytokinesis in bacteria is initiated by polymerization of the tubulin homologue FtsZ into a circular structure at midcell, the Z-ring. This structure functions as a scaffold for all other cell division proteins. Several proteins support assembly of the Z-ring, and one such protein, SepF, is required for normal cell division in Gram-positive bacteria and cyanobacteria. Mutation of sepF results in deformed division septa. It is unclear how SepF contributes to the synthesis of normal septa. We have studied SepF by electron microscopy (EM) and found that the protein assembles into very large (similar to 50nm diameter) rings. These rings were able to bundle FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules. SepF mutants that disturb interaction with FtsZ or that impair ring formation are no longer able to align FtsZ filaments in vitro, and fail to support normal cell division in vivo. We propose that SepF rings are required for the regular arrangement of FtsZ filaments. Absence of this ordered state could explain the grossly distorted septal morphologies seen in sepF mutants. The EMBO Journal (2011) 30, 617-626. doi:10.1038/emboj.2010.345; Published online 11 January 2011


Publication metadata

Author(s): Gündoğdu ME, Kawai Y, Pavlendova N, Ogasawara N, Errington J, Scheffers DJ, Hamoen LW

Publication type: Article

Publication status: Published

Journal: EMBO Journal

Year: 2011

Volume: 30

Issue: 3

Pages: 617-626

Print publication date: 11/01/2011

Date deposited: 09/04/2013

ISSN (print): 0261-4189

ISSN (electronic): 1460-2075

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1038/emboj.2010.345

DOI: 10.1038/emboj.2010.345


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