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  • The EMBO Journal (2009) 28, 2272 - 2282
  • doi:10.1038/emboj.2009.129

Published online: 28 May 2009

Localisation of DivIVA by targeting to negatively curved membranesEMBO Open

Rok Lenarcic1, Sven Halbedel1, Loek Visser1, Michael Shaw2, Ling Juan Wu1, Jeff Errington1, Davide Marenduzzo3 and Leendert W Hamoen1

  1. Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle upon Tyne, UK
  2. Sir William Dunn School of Pathology, University of Oxford, Oxford, UK
  3. Scottish Universities of Physics Alliance, School of Physics, University of Edinburgh, Mayfield Road, Edinburgh, UK

Correspondence to:

Davide Marenduzzo, Scottish Universities of Physics Alliance, School of Physics, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JZ, UK. Tel.: +44 131 650 5289; Fax: +44 131 650 5902; E-mail: dmarendu@ph.ed.ac.uk

Leendert W Hamoen, Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, University of Newcastle, Framlington Place, Newcastle upon Tyne NE2 4HH, UK. Tel.: +44 191 222 8983; Fax: +44 191 222 7424; E-mail: l.hamoen@ncl.ac.uk

Received 28 November 2008; Accepted 15 April 2009

DivIVA is a conserved protein in Gram-positive bacteria and involved in various processes related to cell growth, cell division and spore formation. DivIVA is specifically targeted to cell division sites and cell poles. In Bacillus subtilis, DivIVA helps to localise other proteins, such as the conserved cell division inhibitor proteins, MinC/MinD, and the chromosome segregation protein, RacA. Little is known about the mechanism that localises DivIVA. Here we show that DivIVA binds to liposomes, and that the N terminus harbours the membrane targeting sequence. The purified protein can stimulate binding of RacA to membranes. In mutants with aberrant cell shapes, DivIVA accumulates where the cell membrane is most strongly curved. On the basis of electron microscopic studies and other data, we propose that this is due to molecular bridging of the curvature by DivIVA multimers. This model may explain why DivIVA localises at cell division sites. A Monte-Carlo simulation study showed that molecular bridging can be a general mechanism for binding of proteins to negatively curved membranes.

  • Keywords:

    • Bacillus subtilis,
    • cell division,
    • DivIVA,
    • membrane curvature,
    • phospholipids

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The EMBO Journal is published by Nature Publishing Group on behalf of European Molecular Biology Organization