Conference Proceedings

MinCD cell division proteins form alternating copolymeric cytomotive filaments

Debnath Ghosal, Daniel Trambaiolo, Linda A Amos, Jan Loewe

Nature Communications | NATURE PUBLISHING GROUP | Published : 2014

Abstract

During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imagi..

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Grants

Awarded by Medical Research Council


Awarded by Wellcome Trust


Funding Acknowledgements

We acknowledge support at beamlines id23eh1 and id23eh2 (ESRF, Grenoble, France). minB<SUP>-</SUP> and minB<SUP>-</SUP> slmA<SUP>-</SUP> strains were kind gifts from Thomas G. Bernhardt (Harvard, USA) and strain AB1157 was kindly provided by David Sherratt (Oxford, UK). We thank Joe Lutkenhaus (pJB210: minB), Petra Schwille (EGFP-MinC), Kiyoshi Mizuuchi (EGFP-MinD) and Johan Paulsson (msfGFP) for providing us with plasmids. We thank Thierry Izore, Shaoxia Chen and Christos Savva (MRC-LMB) for help with EM. Work on LMB's FEI Krios microscope was aided by Qing Wang (FEI). This work was supported by the Medical Research Council (U105184326) and the Wellcome Trust (095514/Z/11/Z to J.L.).