Oligomerization of the Bacillus subtilis division protein DivIVA

  1. Lookup NU author(s)
  2. Dr David Scott
  3. Professor Rick Lewis
Author(s)Muchová K, Kutejová E, Scott DJ, Brannigan JA, Lewis RJ, Wilkinson AJ, Barák I
Publication type Article
ISSN (print)1350-0872
ISSN (electronic)1465-2080
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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.
PublisherSociety for General Microbiology
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