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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2016
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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 |
format | Online Article Text |
id | pubmed-5217063 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
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 AT dekkercees mappingoutminproteinpatternsinfullyconfinedfluidicchambers |