Abstract
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.
MeSH Terms
Adenosine Triphosphatases/chemistry,physiology
Adenosine Triphosphate/metabolism
Cell Cycle Proteins
Cell Polarity
Escherichia coli/chemistry,cytology,physiology
Escherichia coli Proteins/chemistry,physiology
Hydrolysis
Oscillometry
Protein Conformation
Chemicals
Cell Cycle Proteins
Escherichia coli Proteins
MinE protein, E coli
Adenosine Triphosphate
Adenosine Triphosphatases
MinD protein, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Huang Kerwyn Casey
Department of Physics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Room 12-111, Cambridge, MA 02139, USA. kch23@mit.edu
Meir Yigal
Wingreen Ned S
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