Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation.
The rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior...
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Series: | PLoS Computational Biology |
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doaj-d75ccc7d954948e6ac0f62ae619df82d2021-04-21T15:36:44ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582013-01-01912e100334710.1371/journal.pcbi.1003347Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation.Mike BonnyElisabeth Fischer-FriedrichMartin LoosePetra SchwilleKarsten KruseThe rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior, which emerges from the interaction of the ATPase MinD and its activator MinE on the cell membrane, has become a paradigm for protein self-organization. Recently, it has been found that not only the binding of MinD to the membrane, but also interactions of MinE with the membrane contribute to Min-protein self-organization. Here, we show that by accounting for this finding in a computational model, we can comprehensively describe all observed Min-protein patterns in vivo and in vitro. Furthermore, by varying the system's geometry, our computations predict patterns that have not yet been reported. We confirm these predictions experimentally.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24339757/pdf/?tool=EBI |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mike Bonny Elisabeth Fischer-Friedrich Martin Loose Petra Schwille Karsten Kruse |
spellingShingle |
Mike Bonny Elisabeth Fischer-Friedrich Martin Loose Petra Schwille Karsten Kruse Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. PLoS Computational Biology |
author_facet |
Mike Bonny Elisabeth Fischer-Friedrich Martin Loose Petra Schwille Karsten Kruse |
author_sort |
Mike Bonny |
title |
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. |
title_short |
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. |
title_full |
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. |
title_fullStr |
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. |
title_full_unstemmed |
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation. |
title_sort |
membrane binding of mine allows for a comprehensive description of min-protein pattern formation. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Computational Biology |
issn |
1553-734X 1553-7358 |
publishDate |
2013-01-01 |
description |
The rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior, which emerges from the interaction of the ATPase MinD and its activator MinE on the cell membrane, has become a paradigm for protein self-organization. Recently, it has been found that not only the binding of MinD to the membrane, but also interactions of MinE with the membrane contribute to Min-protein self-organization. Here, we show that by accounting for this finding in a computational model, we can comprehensively describe all observed Min-protein patterns in vivo and in vitro. Furthermore, by varying the system's geometry, our computations predict patterns that have not yet been reported. We confirm these predictions experimentally. |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24339757/pdf/?tool=EBI |
work_keys_str_mv |
AT mikebonny membranebindingofmineallowsforacomprehensivedescriptionofminproteinpatternformation AT elisabethfischerfriedrich membranebindingofmineallowsforacomprehensivedescriptionofminproteinpatternformation AT martinloose membranebindingofmineallowsforacomprehensivedescriptionofminproteinpatternformation AT petraschwille membranebindingofmineallowsforacomprehensivedescriptionofminproteinpatternformation AT karstenkruse membranebindingofmineallowsforacomprehensivedescriptionofminproteinpatternformation |
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1714667326043848704 |