Browse by author
Lookup NU author(s): Dr David Scott,
Professor Rick Lewis
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Muchová K, Kutejová E, Scott DJ, Brannigan JA, Lewis RJ, Wilkinson AJ, Barák I
Publication type: Article
Publication status: Published
ISSN (print): 1350-0872
ISSN (electronic): 1465-2080
Publisher: Society for General Microbiology