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The distributions of many proteins in rod-shaped bacteria are far fromhomogenous. Often they accumulate at the cell poles or in the cell center. Atthe same time, the copy number of proteins in a single cell is relatively smallmaking the patterns noisy. To explore limits to protein patterns due tomolecular noise, we studied a generic mechanism for spontaneous polar proteinassemblies in rod-shaped bacteria, which is based on cooperative binding ofproteins to the cytoplasmic membrane. For mono-polar assemblies, we find thatthe switching time between the two poles increases exponentially with the celllength and with the protein number.

Bistable protein distributions in rod-shaped bacteria