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Mapping out Min protein patterns in fully confined fluidic chambers

The bacterial Min protein system provides a major model system for studying reaction-diffusion processes in biology. Here we present the first in vitro study of the Min system in fully confined three-dimensional chambers that are lithography-defined, lipid-bilayer coated and isolated through pressur...

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Autores principales: Caspi, Yaron, Dekker, Cees
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217063/
https://www.ncbi.nlm.nih.gov/pubmed/27885986
http://dx.doi.org/10.7554/eLife.19271
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author Caspi, Yaron
Dekker, Cees
author_facet Caspi, Yaron
Dekker, Cees
author_sort Caspi, Yaron
collection PubMed
description The bacterial Min protein system provides a major model system for studying reaction-diffusion processes in biology. Here we present the first in vitro study of the Min system in fully confined three-dimensional chambers that are lithography-defined, lipid-bilayer coated and isolated through pressure valves. We identify three typical dynamical behaviors that occur dependent on the geometrical chamber parameters: pole-to-pole oscillations, spiral rotations, and traveling waves. We establish the geometrical selection rules and show that, surprisingly, Min-protein spiral rotations govern the larger part of the geometrical phase diagram. Confinement as well as an elevated temperature reduce the characteristic wavelength of the Min patterns, although even for confined chambers with a bacterial-level viscosity, the patterns retain a ~5 times larger wavelength than in vivo. Our results provide an essential experimental base for modeling of intracellular Min gradients in bacterial cell division as well as, more generally, for understanding pattern formation in reaction-diffusion systems. DOI: http://dx.doi.org/10.7554/eLife.19271.001
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spelling pubmed-52170632017-01-09 Mapping out Min protein patterns in fully confined fluidic chambers Caspi, Yaron Dekker, Cees eLife Biophysics and Structural Biology The bacterial Min protein system provides a major model system for studying reaction-diffusion processes in biology. Here we present the first in vitro study of the Min system in fully confined three-dimensional chambers that are lithography-defined, lipid-bilayer coated and isolated through pressure valves. We identify three typical dynamical behaviors that occur dependent on the geometrical chamber parameters: pole-to-pole oscillations, spiral rotations, and traveling waves. We establish the geometrical selection rules and show that, surprisingly, Min-protein spiral rotations govern the larger part of the geometrical phase diagram. Confinement as well as an elevated temperature reduce the characteristic wavelength of the Min patterns, although even for confined chambers with a bacterial-level viscosity, the patterns retain a ~5 times larger wavelength than in vivo. Our results provide an essential experimental base for modeling of intracellular Min gradients in bacterial cell division as well as, more generally, for understanding pattern formation in reaction-diffusion systems. DOI: http://dx.doi.org/10.7554/eLife.19271.001 eLife Sciences Publications, Ltd 2016-11-25 /pmc/articles/PMC5217063/ /pubmed/27885986 http://dx.doi.org/10.7554/eLife.19271 Text en © 2016, Caspi et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biophysics and Structural Biology
Caspi, Yaron
Dekker, Cees
Mapping out Min protein patterns in fully confined fluidic chambers
title Mapping out Min protein patterns in fully confined fluidic chambers
title_full Mapping out Min protein patterns in fully confined fluidic chambers
title_fullStr Mapping out Min protein patterns in fully confined fluidic chambers
title_full_unstemmed Mapping out Min protein patterns in fully confined fluidic chambers
title_short Mapping out Min protein patterns in fully confined fluidic chambers
title_sort mapping out min protein patterns in fully confined fluidic chambers
topic Biophysics and Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217063/
https://www.ncbi.nlm.nih.gov/pubmed/27885986
http://dx.doi.org/10.7554/eLife.19271
work_keys_str_mv AT caspiyaron mappingoutminproteinpatternsinfullyconfinedfluidicchambers
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