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Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro
Self-organisation of Min proteins is responsible for the spatial control of cell division in Escherichia coli, and has been studied both in vivo and in vitro. Intriguingly, the protein patterns observed in these settings differ qualitatively and quantitatively. This puzzling dichotomy has not been r...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8175580/ https://www.ncbi.nlm.nih.gov/pubmed/34083526 http://dx.doi.org/10.1038/s41467-021-23412-5 |
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author | Brauns, Fridtjof Pawlik, Grzegorz Halatek, Jacob Kerssemakers, Jacob Frey, Erwin Dekker, Cees |
author_facet | Brauns, Fridtjof Pawlik, Grzegorz Halatek, Jacob Kerssemakers, Jacob Frey, Erwin Dekker, Cees |
author_sort | Brauns, Fridtjof |
collection | PubMed |
description | Self-organisation of Min proteins is responsible for the spatial control of cell division in Escherichia coli, and has been studied both in vivo and in vitro. Intriguingly, the protein patterns observed in these settings differ qualitatively and quantitatively. This puzzling dichotomy has not been resolved to date. Using reconstituted proteins in laterally wide microchambers with a well-controlled height, we experimentally show that the Min protein dynamics on the membrane crucially depend on the micro chamber height due to bulk concentration gradients orthogonal to the membrane. A theoretical analysis shows that in vitro patterns at low microchamber height are driven by the same lateral oscillation mode as pole-to-pole oscillations in vivo. At larger microchamber height, additional vertical oscillation modes set in, marking the transition to a qualitatively different in vitro regime. Our work reveals the qualitatively different mechanisms of mass transport that govern Min protein-patterns for different bulk heights and thus shows that Min patterns in cells are governed by a different mechanism than those in vitro. |
format | Online Article Text |
id | pubmed-8175580 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-81755802021-06-07 Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro Brauns, Fridtjof Pawlik, Grzegorz Halatek, Jacob Kerssemakers, Jacob Frey, Erwin Dekker, Cees Nat Commun Article Self-organisation of Min proteins is responsible for the spatial control of cell division in Escherichia coli, and has been studied both in vivo and in vitro. Intriguingly, the protein patterns observed in these settings differ qualitatively and quantitatively. This puzzling dichotomy has not been resolved to date. Using reconstituted proteins in laterally wide microchambers with a well-controlled height, we experimentally show that the Min protein dynamics on the membrane crucially depend on the micro chamber height due to bulk concentration gradients orthogonal to the membrane. A theoretical analysis shows that in vitro patterns at low microchamber height are driven by the same lateral oscillation mode as pole-to-pole oscillations in vivo. At larger microchamber height, additional vertical oscillation modes set in, marking the transition to a qualitatively different in vitro regime. Our work reveals the qualitatively different mechanisms of mass transport that govern Min protein-patterns for different bulk heights and thus shows that Min patterns in cells are governed by a different mechanism than those in vitro. Nature Publishing Group UK 2021-06-03 /pmc/articles/PMC8175580/ /pubmed/34083526 http://dx.doi.org/10.1038/s41467-021-23412-5 Text en © The Author(s) 2021, corrected publication 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Brauns, Fridtjof Pawlik, Grzegorz Halatek, Jacob Kerssemakers, Jacob Frey, Erwin Dekker, Cees Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title | Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title_full | Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title_fullStr | Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title_full_unstemmed | Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title_short | Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro |
title_sort | bulk-surface coupling identifies the mechanistic connection between min-protein patterns in vivo and in vitro |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8175580/ https://www.ncbi.nlm.nih.gov/pubmed/34083526 http://dx.doi.org/10.1038/s41467-021-23412-5 |
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