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Multistability and dynamic transitions of intracellular Min protein patterns
Cells owe their internal organization to self‐organized protein patterns, which originate and adapt to growth and external stimuli via a process that is as complex as it is little understood. Here, we study the emergence, stability, and state transitions of multistable Min protein oscillation patter...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4923923/ https://www.ncbi.nlm.nih.gov/pubmed/27279643 http://dx.doi.org/10.15252/msb.20156724 |
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author | Wu, Fabai Halatek, Jacob Reiter, Matthias Kingma, Enzo Frey, Erwin Dekker, Cees |
author_facet | Wu, Fabai Halatek, Jacob Reiter, Matthias Kingma, Enzo Frey, Erwin Dekker, Cees |
author_sort | Wu, Fabai |
collection | PubMed |
description | Cells owe their internal organization to self‐organized protein patterns, which originate and adapt to growth and external stimuli via a process that is as complex as it is little understood. Here, we study the emergence, stability, and state transitions of multistable Min protein oscillation patterns in live Escherichia coli bacteria during growth up to defined large dimensions. De novo formation of patterns from homogenous starting conditions is observed and studied both experimentally and in simulations. A new theoretical approach is developed for probing pattern stability under perturbations. Quantitative experiments and simulations show that, once established, Min oscillations tolerate a large degree of intracellular heterogeneity, allowing distinctly different patterns to persist in different cells with the same geometry. Min patterns maintain their axes for hours in experiments, despite imperfections, expansion, and changes in cell shape during continuous cell growth. Transitions between multistable Min patterns are found to be rare events induced by strong intracellular perturbations. The instances of multistability studied here are the combined outcome of boundary growth and strongly nonlinear kinetics, which are characteristic of the reaction–diffusion patterns that pervade biology at many scales. |
format | Online Article Text |
id | pubmed-4923923 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49239232016-07-11 Multistability and dynamic transitions of intracellular Min protein patterns Wu, Fabai Halatek, Jacob Reiter, Matthias Kingma, Enzo Frey, Erwin Dekker, Cees Mol Syst Biol Articles Cells owe their internal organization to self‐organized protein patterns, which originate and adapt to growth and external stimuli via a process that is as complex as it is little understood. Here, we study the emergence, stability, and state transitions of multistable Min protein oscillation patterns in live Escherichia coli bacteria during growth up to defined large dimensions. De novo formation of patterns from homogenous starting conditions is observed and studied both experimentally and in simulations. A new theoretical approach is developed for probing pattern stability under perturbations. Quantitative experiments and simulations show that, once established, Min oscillations tolerate a large degree of intracellular heterogeneity, allowing distinctly different patterns to persist in different cells with the same geometry. Min patterns maintain their axes for hours in experiments, despite imperfections, expansion, and changes in cell shape during continuous cell growth. Transitions between multistable Min patterns are found to be rare events induced by strong intracellular perturbations. The instances of multistability studied here are the combined outcome of boundary growth and strongly nonlinear kinetics, which are characteristic of the reaction–diffusion patterns that pervade biology at many scales. John Wiley and Sons Inc. 2016-06-08 /pmc/articles/PMC4923923/ /pubmed/27279643 http://dx.doi.org/10.15252/msb.20156724 Text en © 2016 The Authors. Published under the terms of the CC BY 4.0 license This is an open access article under the terms of the Creative Commons Attribution 4.0 (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Wu, Fabai Halatek, Jacob Reiter, Matthias Kingma, Enzo Frey, Erwin Dekker, Cees Multistability and dynamic transitions of intracellular Min protein patterns |
title | Multistability and dynamic transitions of intracellular Min protein patterns |
title_full | Multistability and dynamic transitions of intracellular Min protein patterns |
title_fullStr | Multistability and dynamic transitions of intracellular Min protein patterns |
title_full_unstemmed | Multistability and dynamic transitions of intracellular Min protein patterns |
title_short | Multistability and dynamic transitions of intracellular Min protein patterns |
title_sort | multistability and dynamic transitions of intracellular min protein patterns |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4923923/ https://www.ncbi.nlm.nih.gov/pubmed/27279643 http://dx.doi.org/10.15252/msb.20156724 |
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