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In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins
Recent evidence suggests that cells employ functionally asymmetric partitioning schemes in division to cope with aging. We explore various schemes in silico, with a stochastic model of Escherichia coli that includes gene expression, non-functional proteins generation, aggregation and polar retention...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
IOS Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4923715/ https://www.ncbi.nlm.nih.gov/pubmed/25318468 http://dx.doi.org/10.3233/ISB-140462 |
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author | Gupta, Abhishekh Lloyd-Price, Jason Ribeiro, Andre S. |
author_facet | Gupta, Abhishekh Lloyd-Price, Jason Ribeiro, Andre S. |
author_sort | Gupta, Abhishekh |
collection | PubMed |
description | Recent evidence suggests that cells employ functionally asymmetric partitioning schemes in division to cope with aging. We explore various schemes in silico, with a stochastic model of Escherichia coli that includes gene expression, non-functional proteins generation, aggregation and polar retention, and molecule partitioning in division. The model is implemented in SGNS2, which allows stochastic, multi-delayed reactions within hierarchical, transient, interlinked compartments. After setting parameter values of non-functional proteins’ generation and effects that reproduce realistic intracellular and population dynamics, we investigate how the spatial organization of non-functional proteins affects mean division times of cell populations in lineages and, thus, mean cell numbers over time. We find that division times decrease for increasingly asymmetric partitioning. Also, increasing the clustering of non-functional proteins decreases division times. Increasing the bias in polar segregation further decreases division times, particularly if the bias favors the older pole and aggregates’ polar retention is robust. Finally, we show that the non-energy consuming retention of inherited non-functional proteins at the older pole via nucleoid occlusion is a source of functional asymmetries and, thus, is advantageous. Our results suggest that the mechanisms of intracellular organization of non-functional proteins, including clustering and polar retention, affect the vitality of E. coli populations. |
format | Online Article Text |
id | pubmed-4923715 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | IOS Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-49237152016-06-29 In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins Gupta, Abhishekh Lloyd-Price, Jason Ribeiro, Andre S. In Silico Biol Research Article Recent evidence suggests that cells employ functionally asymmetric partitioning schemes in division to cope with aging. We explore various schemes in silico, with a stochastic model of Escherichia coli that includes gene expression, non-functional proteins generation, aggregation and polar retention, and molecule partitioning in division. The model is implemented in SGNS2, which allows stochastic, multi-delayed reactions within hierarchical, transient, interlinked compartments. After setting parameter values of non-functional proteins’ generation and effects that reproduce realistic intracellular and population dynamics, we investigate how the spatial organization of non-functional proteins affects mean division times of cell populations in lineages and, thus, mean cell numbers over time. We find that division times decrease for increasingly asymmetric partitioning. Also, increasing the clustering of non-functional proteins decreases division times. Increasing the bias in polar segregation further decreases division times, particularly if the bias favors the older pole and aggregates’ polar retention is robust. Finally, we show that the non-energy consuming retention of inherited non-functional proteins at the older pole via nucleoid occlusion is a source of functional asymmetries and, thus, is advantageous. Our results suggest that the mechanisms of intracellular organization of non-functional proteins, including clustering and polar retention, affect the vitality of E. coli populations. IOS Press 2015-07-03 /pmc/articles/PMC4923715/ /pubmed/25318468 http://dx.doi.org/10.3233/ISB-140462 Text en IOS Press and the authors. All rights reserved https://creativecommons.org/licenses/by-nc/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial (CC BY-NC 4.0) License (https://creativecommons.org/licenses/by-nc/4.0/) , which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Gupta, Abhishekh Lloyd-Price, Jason Ribeiro, Andre S. In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title |
In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title_full |
In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title_fullStr |
In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title_full_unstemmed |
In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title_short |
In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
title_sort | in silico analysis of division times of escherichia coli populations as a function of the partitioning scheme of non-functional proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4923715/ https://www.ncbi.nlm.nih.gov/pubmed/25318468 http://dx.doi.org/10.3233/ISB-140462 |
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