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Significance Asymmetric cell division yields two distinct daughter cells by mechanisms that underlie stem cell behavior and cellular diversity in all organisms. The bacteriumCaulobacter crescentus is able to orchestrate this complex process with less than 4,000 genes. This article describes a strategy deployed byCaulobacter where a regulatory protein, PopA, is programed to perform distinct roles based on its subcellular address. We demonstrate that, depending on the availability of a second messenger molecule, PopA adopts either a monomer or dimer form. The two oligomeric forms interact with different partners at the two cell poles, playing a critical role in the degradation of a master transcription factor at one pole and flagellar assembly at the other pole.

A localized adaptor protein performs distinct functions at the Caulobacter cell poles