A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD

Mol Microbiol. 2008 Dec;70(6):1556-69. doi: 10.1111/j.1365-2958.2008.06501.x. Epub 2008 Oct 23.

Abstract

Cell division in bacteria is governed by a complex cytokinetic machinery in which the key player is a tubulin homologue, FtsZ. Most rod-shaped bacteria divide precisely at mid-cell between segregated sister chromosomes. Selection of the correct site for cell division is thought to be determined by two negative regulatory systems: the nucleoid occlusion system, which prevents division in the vicinity of the chromosomes, and the Min system, which prevents inappropriate division at the cell poles. In Bacillus subtilis recruitment of the division inhibitor MinCD to cell poles depends on DivIVA, and these proteins were thought to be sufficient for Min function. We have now identified a novel component of the division-site selection system, MinJ, which bridges DivIVA and MinD. minJ mutants are impaired in division because MinCD activity is no longer restricted to cell poles. Although MinCD was thought to act specifically on FtsZ assembly, analysis of minJ and divIVA mutants showed that their block in division occurs downstream of FtsZ. The results support a model in which the main function of the Min system lies in allowing only a single round of division per cell cycle, and that MinCD acts at multiple levels to prevent inappropriate division.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / cytology
  • Bacillus subtilis / metabolism
  • Bacillus subtilis / physiology*
  • Bacterial Proteins / metabolism*
  • Cell Cycle Proteins / metabolism*
  • Cell Division*
  • Cytoskeletal Proteins / metabolism*

Substances

  • Bacterial Proteins
  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • DivIVA protein, bacteria
  • FtsZ protein, Bacteria
  • MinC protein, Bacteria