Abstract
The Min system of proteins, consisting of MinC, MinD and MinE, is essential for normal cell division in Escherichia coli. MinC forms a polar gradient to restrict placement of the division septum to midcell. MinC localization occurs through a direct interaction with MinD, a membrane-associating Par-like ATPase. MinE stimulates ATP hydrolysis by MinD, thereby releasing MinD from the membrane. Here, we show that MinD forms polymers with MinC and ATP without the addition of phospholipids. The topological regulator MinE induces disassembly of MinCD polymers. Two MinD mutant proteins, MinD(K11A) and MinD(ΔMTS15), are unable to form polymers with MinC.
Keywords:
ATPase; Cytokinesis; Min system; MinE; Phospholipids.
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Adenosine Triphosphatases / ultrastructure
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Adenosine Triphosphate / metabolism*
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Escherichia coli / chemistry
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Escherichia coli / cytology
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Escherichia coli Proteins / ultrastructure
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Membrane Proteins / ultrastructure
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Microbial Viability
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Microscopy, Electron, Transmission
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Models, Molecular
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Protein Multimerization
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Protein Structure, Quaternary
Substances
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Escherichia coli Proteins
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Membrane Proteins
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MinC protein, E coli
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Adenosine Triphosphate
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Adenosine Triphosphatases
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MinD protein, E coli