Oligomerization of the Bacillus subtilis division protein DivIVA (2002)

Author(s): Muchová K, Kutejová E, Scott DJ, Brannigan JA, Lewis RJ, Wilkinson AJ, Barák I

    Abstract: DivIVA appears to be a mediator of inhibition by MinCD of division at the cell poles in Bacillus subtilis. Gel permeation and ultracentrifugation techniques were used to show self-association of DivIVA into a form consisting of 10–12 monomers in vitro. Western blot analysis of non-denaturating polyacrylamide gels confirms the presence of similar oligomers in B. subtilis cell lysates. These oligomers persist in a B. subtilis strain containing the divIVA1 mutation, in which proper vegetative septum positioning is abolished. In contrast, the divIVA2 mutation, which has a similar biological impact, appears to produce a protein with different oligomerization properties. The results of the present study suggest that oligomerization of DivIVA is important, but not sufficient for its function in the cell division process.

      • Date: 01-03-2002
      • Journal: Microbiology
      • Volume: 148
      • Issue: 3
      • Pages: 807-813
      • Publisher: Society for General Microbiology
      • Publication type: Article
      • Bibliographic status: Published

      Keywords: division, blue native electrophoresis, analytical ultracentrifugation, sporulation


      Professor Rick Lewis
      Prof of Structural Biology