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• W1967845172 abstract "Cell polarity is a fundamental feature of all cell types and is essential for cell division, cell migration, and vectorial transport of cell fate determinants within a cell (1). In recent years, application of cytological methods to study protein, chromosome, and episome localization in chemically fixed and live bacterial cells has signaled the advent of prokaryotic cell biology and has provided us with new, sometimes startling, imagery of the spatial organization within a bacterial cell (2). Proteins are found to be positioned at specific sites in bacteria such as the cell pole, the cell equator, and the division septum. Such site-specific protein targeting appears to be central to the regulation of DNA replication, chromosome segregation, cell division, cell differentiation, and chemotaxis. Recent studies on a group of proteins in Escherichia coli , termed Min, have revealed an extraordinary oscillatory behavior that governs their cellular location. The dynamic behavior of the Min proteins creates transient domains of subcellular asymmetry in the E. coli cell and such cell polarization is critical to the ability of the Min system to ensure that a cell divides unerringly in the middle. In a recent issue of PNAS, Fu et al. (3) describe a remarkable cell polarization feature of the MinE protein that localizes as an off-center ring (E-ring) and as a polar zone (PZ) that extends from the ring to the proximal cell pole. Time-lapse microscopy of live E. coli cells expressing a MinE-green fluorescent protein fusion reveals that the membrane-associated E-ring and the PZ form a mobile unit, with the PZ shrinking as the E-ring moves toward the proximal pole. Upon reaching the polar extremity, the PZ and the ring disappear, only to reappear at the opposite pole. The sequence of MinE assembly, poleward movement, dispersion, and reassembly is repeated many times in each …" @default.
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• W1967845172 date "2001-02-13" @default.
• W1967845172 modified "2023-10-18" @default.
• W1967845172 title "Protein acrobatics and bacterial cell polarity" @default.
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• W1967845172 doi "https://doi.org/10.1073/pnas.98.4.1332" @default.
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