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PMID: 14569005 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones.

Huang KC, Meir Y, Wingreen NS

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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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2003-10-28
Epub
2003-00-20
Pages
12724-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC240685
Subset
IM
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