Bacterial cell division proteins must assemble at the middle of the cell to ensure the viability of both daughter cells. The first step in the assembly of the cell division apparatus is the polymerization of the tubulin-like protein FtsZ into a ring-shaped scaffold, the Z-ring. The Min system contributes to the spatial precision of division by inhibiting FtsZ polymerization at the cell poles. The component of this system that interacts with FtsZ is MinC, a 25 kDa protein that has two domains. The N-terminal domain of MinC is the main responsible for FtsZ inhibition, being sufficient to block Z-ring assembly when overexpressed in vivo, and to inhibit FtsZ polymerization in vitro. Despite intensive studies, little is known about the MinC binding site for FtsZ. We have assigned the backbone and side chain resonances of the MinC N-terminal domain of Bacillus subtilis through NMR spectroscopy. These assignments provide the basis to characterize the interaction between the N-terminal domain of MinC and FtsZ by NMR methods.
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