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Polarity of c-di-GMP synthesis and degradation
The bacterial cell pole has long been recognized as a defined compartment for enzymatic activities that are important or even vital for the cell. Polarity of diguanylate cyclases and phosphodiesterases, enzymes that synthesize and degrade the second messenger c-di-GMP, has now been demonstrated for...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212136/ https://www.ncbi.nlm.nih.gov/pubmed/37251513 http://dx.doi.org/10.1093/femsml/uqad014 |
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author | Kreiling, Vanessa Thormann, Kai M |
author_facet | Kreiling, Vanessa Thormann, Kai M |
author_sort | Kreiling, Vanessa |
collection | PubMed |
description | The bacterial cell pole has long been recognized as a defined compartment for enzymatic activities that are important or even vital for the cell. Polarity of diguanylate cyclases and phosphodiesterases, enzymes that synthesize and degrade the second messenger c-di-GMP, has now been demonstrated for several bacterial systems. Here we review these polar regulatory systems and show how the asymmetry of c-di-GMP production and turnover in concert with different modes of activation and deactivation creates heterogeneity in cellular c-di-GMP levels. We highlight how this heterogeneity generates a diverse set of phenotypic identities or states and how this may benefit the cell population, and we discuss reasons why the polarity of c-di-GMP signaling is probably widespread among bacteria. |
format | Online Article Text |
id | pubmed-10212136 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-102121362023-05-26 Polarity of c-di-GMP synthesis and degradation Kreiling, Vanessa Thormann, Kai M Microlife Short Review The bacterial cell pole has long been recognized as a defined compartment for enzymatic activities that are important or even vital for the cell. Polarity of diguanylate cyclases and phosphodiesterases, enzymes that synthesize and degrade the second messenger c-di-GMP, has now been demonstrated for several bacterial systems. Here we review these polar regulatory systems and show how the asymmetry of c-di-GMP production and turnover in concert with different modes of activation and deactivation creates heterogeneity in cellular c-di-GMP levels. We highlight how this heterogeneity generates a diverse set of phenotypic identities or states and how this may benefit the cell population, and we discuss reasons why the polarity of c-di-GMP signaling is probably widespread among bacteria. Oxford University Press 2023-04-05 /pmc/articles/PMC10212136/ /pubmed/37251513 http://dx.doi.org/10.1093/femsml/uqad014 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Short Review Kreiling, Vanessa Thormann, Kai M Polarity of c-di-GMP synthesis and degradation |
title | Polarity of c-di-GMP synthesis and degradation |
title_full | Polarity of c-di-GMP synthesis and degradation |
title_fullStr | Polarity of c-di-GMP synthesis and degradation |
title_full_unstemmed | Polarity of c-di-GMP synthesis and degradation |
title_short | Polarity of c-di-GMP synthesis and degradation |
title_sort | polarity of c-di-gmp synthesis and degradation |
topic | Short Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212136/ https://www.ncbi.nlm.nih.gov/pubmed/37251513 http://dx.doi.org/10.1093/femsml/uqad014 |
work_keys_str_mv | AT kreilingvanessa polarityofcdigmpsynthesisanddegradation AT thormannkaim polarityofcdigmpsynthesisanddegradation |