Publication:
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
- URL: http://mic.sgmjournals.org/cgi/content/abstract/148/3/807
- ISSN (electronic): 1465-2080
Keywords: division, blue native electrophoresis, analytical ultracentrifugation, sporulation
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Professor Rick Lewis
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