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The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis
The core of the chemotaxis system of Shewanella oneidensis is made of the CheA3 kinase and the CheY3 regulator. When appropriated, CheA3 phosphorylates CheY3, which, in turn, binds to the rotor of the flagellum to modify the swimming direction. In this study, we showed that phosphorylated CheY3 (Che...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7666153/ https://www.ncbi.nlm.nih.gov/pubmed/33188190 http://dx.doi.org/10.1038/s41522-020-00165-5 |
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author | Boyeldieu, Anne Ali Chaouche, Amine Ba, Moly Honoré, Flora Ambre Méjean, Vincent Jourlin-Castelli, Cécile |
author_facet | Boyeldieu, Anne Ali Chaouche, Amine Ba, Moly Honoré, Flora Ambre Méjean, Vincent Jourlin-Castelli, Cécile |
author_sort | Boyeldieu, Anne |
collection | PubMed |
description | The core of the chemotaxis system of Shewanella oneidensis is made of the CheA3 kinase and the CheY3 regulator. When appropriated, CheA3 phosphorylates CheY3, which, in turn, binds to the rotor of the flagellum to modify the swimming direction. In this study, we showed that phosphorylated CheY3 (CheY3-P) also plays an essential role during biogenesis of the solid-surface-associated biofilm (SSA-biofilm). Indeed, in a ΔcheY3 strain, the formation of this biofilm is abolished. Using the phospho-mimetic CheY3D56E mutant, we showed that CheY-P is required throughout the biogenesis of the biofilm but CheY3 phosphorylation is independent of CheA3 during this process. We have recently found that CheY3 interacts with two diguanylate cyclases (DGCs) and with MxdA, the c-di-GMP effector, probably triggering exopolysaccharide synthesis by the Mxd machinery. Here, we discovered two additional DGCs involved in SSA-biofilm development and showed that one of them interacts with CheY3. We therefore propose that CheY3-P acts together with DGCs to control SSA-biofilm formation. Interestingly, two orthologous CheY regulators complement the biofilm defect of a ΔcheY3 strain, supporting the idea that biofilm formation could involve CheY regulators in other bacteria. |
format | Online Article Text |
id | pubmed-7666153 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-76661532020-11-16 The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis Boyeldieu, Anne Ali Chaouche, Amine Ba, Moly Honoré, Flora Ambre Méjean, Vincent Jourlin-Castelli, Cécile NPJ Biofilms Microbiomes Article The core of the chemotaxis system of Shewanella oneidensis is made of the CheA3 kinase and the CheY3 regulator. When appropriated, CheA3 phosphorylates CheY3, which, in turn, binds to the rotor of the flagellum to modify the swimming direction. In this study, we showed that phosphorylated CheY3 (CheY3-P) also plays an essential role during biogenesis of the solid-surface-associated biofilm (SSA-biofilm). Indeed, in a ΔcheY3 strain, the formation of this biofilm is abolished. Using the phospho-mimetic CheY3D56E mutant, we showed that CheY-P is required throughout the biogenesis of the biofilm but CheY3 phosphorylation is independent of CheA3 during this process. We have recently found that CheY3 interacts with two diguanylate cyclases (DGCs) and with MxdA, the c-di-GMP effector, probably triggering exopolysaccharide synthesis by the Mxd machinery. Here, we discovered two additional DGCs involved in SSA-biofilm development and showed that one of them interacts with CheY3. We therefore propose that CheY3-P acts together with DGCs to control SSA-biofilm formation. Interestingly, two orthologous CheY regulators complement the biofilm defect of a ΔcheY3 strain, supporting the idea that biofilm formation could involve CheY regulators in other bacteria. Nature Publishing Group UK 2020-11-13 /pmc/articles/PMC7666153/ /pubmed/33188190 http://dx.doi.org/10.1038/s41522-020-00165-5 Text en © The Author(s) 2020 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/. |
spellingShingle | Article Boyeldieu, Anne Ali Chaouche, Amine Ba, Moly Honoré, Flora Ambre Méjean, Vincent Jourlin-Castelli, Cécile The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title | The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title_full | The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title_fullStr | The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title_full_unstemmed | The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title_short | The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis |
title_sort | phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in shewanella oneidensis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7666153/ https://www.ncbi.nlm.nih.gov/pubmed/33188190 http://dx.doi.org/10.1038/s41522-020-00165-5 |
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