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
DOI: 10.1038/ncomms6341
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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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.).