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Research Paper |
Institute of Molecular Biology, Slovak Academy of Sciences, 842 51 Bratislava, Slovakia1
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK2
Department of Biology, University of York, Heslington YO10 5YW, UK3
Author for correspondence: Imrich Barák. Tel: +421 7 5941 2152. Fax: +421 7 5477 2316. e-mail: umbibara{at}savba.sk
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.
Keywords: cell division, blue native electrophoresis, analytical ultracentrifugation, sporulation
Abbreviations: GFP, green fluorescent protein
a Present address: Laboratory of Molecular Biophysics, The Rex Richards Building, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
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