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Tuesday, October 25, 2011 — Poster Session II | |||
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Noon – 2:00 p.m. |
Natcher Conference Center |
NCI |
MOLBIO-3 |
The orchestrated assembly of the cell division machinery at mid-cell is a critical step of cytokinesis. Here, we examined the localization and assembly of the bacterial cell division protein DivIVA, which resembles eukaryotic tropomyosins, in Bacillus subtilis. DivIVA preferentially localizes to highly negatively curved membranes. We report that it forms two distinct structures depending on where it is found: double rings near mid-cell flanking division septa or patches at hemispherical cell poles, and that the particular structure formed by DivIVA is dictated by the cell’s local architecture. We propose a model in which the template-driven assembly of DivIVA rings near nascent septa prevents aberrant septum formation at adjacent sites and properly positions DivIVA patches at the extreme poles when cells growing as chains eventually separate into individual cells. Template-driven assembly may be a widely conserved strategy for the assembly of multifunctional proteins into large structures in a cell architecture-dependent manner.