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Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism
Networks of molecular chaperones maintain cellular protein homeostasis by acting at nearly every step in the biogenesis of proteins and protein complexes. Herein, we demonstrate that the major chaperone DnaK/HSP70 of the model bacterium Escherichia coli is critical for the proper functioning of the...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5269706/ https://www.ncbi.nlm.nih.gov/pubmed/28128357 http://dx.doi.org/10.1038/srep41341 |
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author | Anglès, Fréderic Castanié-Cornet, Marie-Pierre Slama, Nawel Dinclaux, Mickael Cirinesi, Anne-Marie Portais, Jean-Charles Létisse, Fabien Genevaux, Pierre |
author_facet | Anglès, Fréderic Castanié-Cornet, Marie-Pierre Slama, Nawel Dinclaux, Mickael Cirinesi, Anne-Marie Portais, Jean-Charles Létisse, Fabien Genevaux, Pierre |
author_sort | Anglès, Fréderic |
collection | PubMed |
description | Networks of molecular chaperones maintain cellular protein homeostasis by acting at nearly every step in the biogenesis of proteins and protein complexes. Herein, we demonstrate that the major chaperone DnaK/HSP70 of the model bacterium Escherichia coli is critical for the proper functioning of the central metabolism and for the cellular response to carbon nutrition changes, either directly or indirectly via the control of the heat-shock response. We identified carbon sources whose utilization was positively or negatively affected by DnaK and isolated several central metabolism genes (among other genes identified in this work) that compensate for the lack of DnaK and/or DnaK/Trigger Factor chaperone functions in vivo. Using carbon sources with specific entry points coupled to NMR analyses of real-time carbon assimilation, metabolic coproducts production and flux rearrangements, we demonstrate that DnaK significantly impacts the hierarchical order of carbon sources utilization, the excretion of main coproducts and the distribution of metabolic fluxes, thus revealing a multilevel interaction of DnaK with the central metabolism. |
format | Online Article Text |
id | pubmed-5269706 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52697062017-02-01 Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism Anglès, Fréderic Castanié-Cornet, Marie-Pierre Slama, Nawel Dinclaux, Mickael Cirinesi, Anne-Marie Portais, Jean-Charles Létisse, Fabien Genevaux, Pierre Sci Rep Article Networks of molecular chaperones maintain cellular protein homeostasis by acting at nearly every step in the biogenesis of proteins and protein complexes. Herein, we demonstrate that the major chaperone DnaK/HSP70 of the model bacterium Escherichia coli is critical for the proper functioning of the central metabolism and for the cellular response to carbon nutrition changes, either directly or indirectly via the control of the heat-shock response. We identified carbon sources whose utilization was positively or negatively affected by DnaK and isolated several central metabolism genes (among other genes identified in this work) that compensate for the lack of DnaK and/or DnaK/Trigger Factor chaperone functions in vivo. Using carbon sources with specific entry points coupled to NMR analyses of real-time carbon assimilation, metabolic coproducts production and flux rearrangements, we demonstrate that DnaK significantly impacts the hierarchical order of carbon sources utilization, the excretion of main coproducts and the distribution of metabolic fluxes, thus revealing a multilevel interaction of DnaK with the central metabolism. Nature Publishing Group 2017-01-27 /pmc/articles/PMC5269706/ /pubmed/28128357 http://dx.doi.org/10.1038/srep41341 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Anglès, Fréderic Castanié-Cornet, Marie-Pierre Slama, Nawel Dinclaux, Mickael Cirinesi, Anne-Marie Portais, Jean-Charles Létisse, Fabien Genevaux, Pierre Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title | Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title_full | Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title_fullStr | Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title_full_unstemmed | Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title_short | Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism |
title_sort | multilevel interaction of the dnak/dnaj(hsp70/hsp40) stress-responsive chaperone machine with the central metabolism |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5269706/ https://www.ncbi.nlm.nih.gov/pubmed/28128357 http://dx.doi.org/10.1038/srep41341 |
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