The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.
Placement of the division site at midcell in Escherichia coli requires the MinE protein. MinE acts by imparting topological specificity to the MinCD division inhibitor, preventing the inhibitor from acting at the midcell site while permitting it to block division at other unwanted sites along the length of the cell. It was previously shown that MinE assembled into a ring structure that appeared to be localized near midcell, apparently explaining the ability of MinE to specifically counteract MinCD at midcell. We report here that the MinE ring is not fixed in position near midcell but is a dynamic structure that undergoes a repetitive cycle of movement first to one cell pole and then to the opposite pole. Taken together with studies of the dynamic behavior of the MinD protein, the results suggest that the topological specificity of division site placement may not involve a localized action of MinE to counteract the MinCD division inhibitor at midcell but rather the ability of MinE to move the division inhibitor away from midcell and to the cell poles.
Fu
X
X
Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06030, USA.
Shih
Y L
YL
Zhang
Y
Y
Rothfield
L I
LI
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D002453:Cell Cycle / Q000502:physiology; D018797:Cell Cycle Proteins; D016764:Cell Polarity; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D021381:Protein Transport
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C080466:MinC protein, Bacteria; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli