Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones.
In Escherichia coli, division site selection is regulated in part by the Min-protein system. Oscillations of the Min proteins from pole to pole every approximately 40 sec have been revealed by in vivo studies of GFP fusions. The dynamic oscillatory structures produced by the Min proteins, including a ring of MinE protein, compact polar zones of MinD, and zebra-striped oscillations in filamentous cells, remain unexplained. We show that the Min oscillations, including mutant phenotypes, can be accounted for by in vitro-observed interactions involving MinD and MinE, with a crucial role played by the rate of nucleotide exchange. Recent discoveries suggest that protein oscillations may play a general role in proper chromosome and plasmid partitioning.
Huang
Kerwyn Casey
KC
Department of Physics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Room 12-111, Cambridge, MA 02139, USA. kch23@mit.edu
Meir
Yigal
Y
Wingreen
Ned S
NS
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000502:physiology; D000255:Adenosine Triphosphate / Q000378:metabolism; D018797:Cell Cycle Proteins; D016764:Cell Polarity; D004926:Escherichia coli / Q000737:chemistry* / Q000166:cytology / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology; D006868:Hydrolysis; D009991:Oscillometry; D011487:Protein Conformation
D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C093548:MinE protein, E coli; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli