Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site

Genes Dev. 1998 Nov 1;12(21):3419-30. doi: 10.1101/gad.12.21.3419.


Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphatases / physiology*
  • Bacillus subtilis / physiology*
  • Bacterial Proteins / physiology
  • Cell Cycle Proteins / metabolism
  • Cell Cycle Proteins / physiology
  • Cell Division / physiology
  • Cell Polarity / physiology
  • Escherichia coli Proteins*
  • Green Fluorescent Proteins
  • Luminescent Proteins / genetics
  • Microscopy, Fluorescence
  • Models, Biological
  • Recombinant Fusion Proteins / genetics


  • Bacterial Proteins
  • Cell Cycle Proteins
  • DivIVA protein, bacteria
  • Escherichia coli Proteins
  • Luminescent Proteins
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Adenosine Triphosphatases
  • MinD protein, E coli