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Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations

Better understanding of uranyl toxicity in bacteria is necessary to optimize strains for bioremediation purposes or for using bacteria as biodetectors for bioavailable uranyl. In this study, after different steps of optimization, Escherichia colicells were exposed to uranyl at low pH to minimize ura...

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Autores principales: Khemiri, Arbia, Carrière, Marie, Bremond, Nicolas, Ben Mlouka, Mohamed Amine, Coquet, Laurent, Llorens, Isabelle, Chapon, Virginie, Jouenne, Thierry, Cosette, Pascal, Berthomieu, Catherine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935937/
https://www.ncbi.nlm.nih.gov/pubmed/24587082
http://dx.doi.org/10.1371/journal.pone.0089863
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author Khemiri, Arbia
Carrière, Marie
Bremond, Nicolas
Ben Mlouka, Mohamed Amine
Coquet, Laurent
Llorens, Isabelle
Chapon, Virginie
Jouenne, Thierry
Cosette, Pascal
Berthomieu, Catherine
author_facet Khemiri, Arbia
Carrière, Marie
Bremond, Nicolas
Ben Mlouka, Mohamed Amine
Coquet, Laurent
Llorens, Isabelle
Chapon, Virginie
Jouenne, Thierry
Cosette, Pascal
Berthomieu, Catherine
author_sort Khemiri, Arbia
collection PubMed
description Better understanding of uranyl toxicity in bacteria is necessary to optimize strains for bioremediation purposes or for using bacteria as biodetectors for bioavailable uranyl. In this study, after different steps of optimization, Escherichia colicells were exposed to uranyl at low pH to minimize uranyl precipitation and to increase its bioavailability. Bacteria were adapted to mid acidic pH before exposure to 50 or 80 µM uranyl acetate for two hours at pH≈3. To evaluate the impact of uranium, growth in these conditions were compared and the same rates of cells survival were observed in control and uranyl exposed cultures. Additionally, this impact was analyzedby two-dimensional differential gel electrophoresis proteomics to discover protein actors specifically present or accumulated in contact with uranium.Exposure to uranium resulted in differential accumulation of proteins associated with oxidative stress and in the accumulation of the NADH/quinone oxidoreductase WrbA. This FMN dependent protein performs obligate two-electron reduction of quinones, and may be involved in cells response to oxidative stress. Interestingly, this WrbA protein presents similarities with the chromate reductase from E. coli, which was shown to reduce uranyl in vitro.
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spelling pubmed-39359372014-03-04 Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations Khemiri, Arbia Carrière, Marie Bremond, Nicolas Ben Mlouka, Mohamed Amine Coquet, Laurent Llorens, Isabelle Chapon, Virginie Jouenne, Thierry Cosette, Pascal Berthomieu, Catherine PLoS One Research Article Better understanding of uranyl toxicity in bacteria is necessary to optimize strains for bioremediation purposes or for using bacteria as biodetectors for bioavailable uranyl. In this study, after different steps of optimization, Escherichia colicells were exposed to uranyl at low pH to minimize uranyl precipitation and to increase its bioavailability. Bacteria were adapted to mid acidic pH before exposure to 50 or 80 µM uranyl acetate for two hours at pH≈3. To evaluate the impact of uranium, growth in these conditions were compared and the same rates of cells survival were observed in control and uranyl exposed cultures. Additionally, this impact was analyzedby two-dimensional differential gel electrophoresis proteomics to discover protein actors specifically present or accumulated in contact with uranium.Exposure to uranium resulted in differential accumulation of proteins associated with oxidative stress and in the accumulation of the NADH/quinone oxidoreductase WrbA. This FMN dependent protein performs obligate two-electron reduction of quinones, and may be involved in cells response to oxidative stress. Interestingly, this WrbA protein presents similarities with the chromate reductase from E. coli, which was shown to reduce uranyl in vitro. Public Library of Science 2014-02-26 /pmc/articles/PMC3935937/ /pubmed/24587082 http://dx.doi.org/10.1371/journal.pone.0089863 Text en © 2014 Khemiri et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Khemiri, Arbia
Carrière, Marie
Bremond, Nicolas
Ben Mlouka, Mohamed Amine
Coquet, Laurent
Llorens, Isabelle
Chapon, Virginie
Jouenne, Thierry
Cosette, Pascal
Berthomieu, Catherine
Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title_full Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title_fullStr Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title_full_unstemmed Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title_short Escherichia coli Response to Uranyl Exposure at Low pH and Associated Protein Regulations
title_sort escherichia coli response to uranyl exposure at low ph and associated protein regulations
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935937/
https://www.ncbi.nlm.nih.gov/pubmed/24587082
http://dx.doi.org/10.1371/journal.pone.0089863
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