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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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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. |
format | Online Article Text |
id | pubmed-3935937 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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