Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli.
Accurate placement of the division septum at the midpoint of Escherichia coli cells requires the combined action of a general division inhibitor (MinC), a site-specific suppressor of division inhibition (MinE), and an ATPase (MinD) that is required for proper functioning of both MinC and MinE. We previously showed that a functional MinE-Gfp fusion accumulates in a ring structure at/near the middle of cells. Here we show that functional Gfp-MinD accumulates alternately in either one of the cell halves in what appears to be a rapidly oscillating membrane association-dissociation cycle imposed by MinE. The results indicate that MinD represents a novel type of dynamic cellular element in bacteria, with multiple roles in directing the division apparatus to the middle of the cell.
Raskin
D M
DM
Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-4960, USA.
de Boer
P A
PA
D000251:Adenosine Triphosphatases / Q000502:physiology*; D001426:Bacterial Proteins / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D004926:Escherichia coli / Q000254:growth & development* / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000502:physiology
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli