Mechanisms Underlying Subcellular Localization of the Bacterial Transmembrane Chemoreceptor

Abstract

The chemoreceptors of Escherichia coli cluster at a cell pole, a property which is critical for signaling. However, little is known about the mechanism of polar localization. Our recent study demonstrated that the aspartate chemoreceptor (Tar)-GFP fusion protein is inserted into lateral membrane regions and migrates to the pole. Unexpectedly, Tar-GFP was found to be arranged into a coil, which reflects a coil of the Sec protein translocation machinery. The Sec coil appeared distinct from the coil of MreB, an actin-like cytoskeletal protein. These findings shed new light on the spatial organization of membrane proteins in E. coli.