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Effects of geometry and topography on Min-protein dynamics

In the rod-shaped bacterium Escherichia coli, the center is selected by the Min-proteins as the site of cell division. To this end, the proteins periodically translocate between the two cell poles, where they suppress assembly of the cell division machinery. Ample evidence notably obtained from in v...

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Detalles Bibliográficos
Autores principales: Wettmann, Lukas, Bonny, Mike, Kruse, Karsten
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6117030/
https://www.ncbi.nlm.nih.gov/pubmed/30161173
http://dx.doi.org/10.1371/journal.pone.0203050
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author Wettmann, Lukas
Bonny, Mike
Kruse, Karsten
author_facet Wettmann, Lukas
Bonny, Mike
Kruse, Karsten
author_sort Wettmann, Lukas
collection PubMed
description In the rod-shaped bacterium Escherichia coli, the center is selected by the Min-proteins as the site of cell division. To this end, the proteins periodically translocate between the two cell poles, where they suppress assembly of the cell division machinery. Ample evidence notably obtained from in vitro reconstitution experiments suggests that the oscillatory pattern results from self-organization of the proteins MinD and MinE in presence of a membrane. A mechanism built on cooperative membrane attachment of MinD and persistent MinD removal from the membrane induced by MinE has been shown to be able to reproduce the observed Min-protein patterns in rod-shaped E. coli and on flat supported lipid bilayers. Here, we report our results of a numerical investigation of patterns generated by this mechanism in various geoemtries. Notably, we consider the dynamics on membrane patches of different forms, on topographically structured lipid bilayers, and in closed geometries of various shapes. We find that all previously described patterns can be reproduced by the mechanism. However, it requires different parameter sets for reproducing the patterns in closed and in open geometries.
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spelling pubmed-61170302018-09-16 Effects of geometry and topography on Min-protein dynamics Wettmann, Lukas Bonny, Mike Kruse, Karsten PLoS One Research Article In the rod-shaped bacterium Escherichia coli, the center is selected by the Min-proteins as the site of cell division. To this end, the proteins periodically translocate between the two cell poles, where they suppress assembly of the cell division machinery. Ample evidence notably obtained from in vitro reconstitution experiments suggests that the oscillatory pattern results from self-organization of the proteins MinD and MinE in presence of a membrane. A mechanism built on cooperative membrane attachment of MinD and persistent MinD removal from the membrane induced by MinE has been shown to be able to reproduce the observed Min-protein patterns in rod-shaped E. coli and on flat supported lipid bilayers. Here, we report our results of a numerical investigation of patterns generated by this mechanism in various geoemtries. Notably, we consider the dynamics on membrane patches of different forms, on topographically structured lipid bilayers, and in closed geometries of various shapes. We find that all previously described patterns can be reproduced by the mechanism. However, it requires different parameter sets for reproducing the patterns in closed and in open geometries. Public Library of Science 2018-08-30 /pmc/articles/PMC6117030/ /pubmed/30161173 http://dx.doi.org/10.1371/journal.pone.0203050 Text en © 2018 Wettmann et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Wettmann, Lukas
Bonny, Mike
Kruse, Karsten
Effects of geometry and topography on Min-protein dynamics
title Effects of geometry and topography on Min-protein dynamics
title_full Effects of geometry and topography on Min-protein dynamics
title_fullStr Effects of geometry and topography on Min-protein dynamics
title_full_unstemmed Effects of geometry and topography on Min-protein dynamics
title_short Effects of geometry and topography on Min-protein dynamics
title_sort effects of geometry and topography on min-protein dynamics
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6117030/
https://www.ncbi.nlm.nih.gov/pubmed/30161173
http://dx.doi.org/10.1371/journal.pone.0203050
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