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 ≈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 Min...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2003-10, Vol.100 (22), p.12724-12728
Main Authors: Huang, Kerwyn Casey, Meir, Yigal, Wingreen, Ned S.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - physiology
Adenosine Triphosphate - metabolism
Bacteria
Biological Sciences
Cell Cycle Proteins
Cell division
Cell membranes
Cell Polarity
Cellular biology
Cytoplasm
Daughter cells
Escherichia coli
Escherichia coli - chemistry
Escherichia coli - cytology
Escherichia coli - physiology
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - physiology
Hydrolysis
Mental concentration
Mining
Nucleotides
Oscillation
Oscillometry
Protein Conformation
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Summary: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 ≈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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2135445100