Oligomerization of the Bacillus subtilis division protein DivIVA

Microbiology (Reading). 2002 Mar;148(Pt 3):807-813. doi: 10.1099/00221287-148-3-807.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Dimerization
  • Electrophoresis, Polyacrylamide Gel / methods
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Mutation
  • Rosaniline Dyes
  • Ultracentrifugation

Substances

  • Bacterial Proteins
  • Cell Cycle Proteins
  • DivIVA protein, bacteria
  • Rosaniline Dyes
  • Coomassie blue