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 coli cells were exposed to uranyl at low pH to minimize ur...

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Main Authors: Arbia Khemiri, Marie Carrière, Nicolas Bremond, Mohamed Amine Ben Mlouka, Laurent Coquet, Isabelle Llorens, Virginie Chapon, Thierry Jouenne, Pascal Cosette, Catherine Berthomieu
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3935937?pdf=render
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spelling doaj-4a535c0d9e1543ccbe2fb7a39d3701d52020-11-24T21:42:53ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0192e8986310.1371/journal.pone.0089863Escherichia coli response to uranyl exposure at low pH and associated protein regulations.Arbia KhemiriMarie CarrièreNicolas BremondMohamed Amine Ben MloukaLaurent CoquetIsabelle LlorensVirginie ChaponThierry JouennePascal CosetteCatherine BerthomieuBetter 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 coli cells 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 analyzed by 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.http://europepmc.org/articles/PMC3935937?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Arbia Khemiri
Marie Carrière
Nicolas Bremond
Mohamed Amine Ben Mlouka
Laurent Coquet
Isabelle Llorens
Virginie Chapon
Thierry Jouenne
Pascal Cosette
Catherine Berthomieu
spellingShingle Arbia Khemiri
Marie Carrière
Nicolas Bremond
Mohamed Amine Ben Mlouka
Laurent Coquet
Isabelle Llorens
Virginie Chapon
Thierry Jouenne
Pascal Cosette
Catherine Berthomieu
Escherichia coli response to uranyl exposure at low pH and associated protein regulations.
PLoS ONE
author_facet Arbia Khemiri
Marie Carrière
Nicolas Bremond
Mohamed Amine Ben Mlouka
Laurent Coquet
Isabelle Llorens
Virginie Chapon
Thierry Jouenne
Pascal Cosette
Catherine Berthomieu
author_sort Arbia Khemiri
title 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_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_sort escherichia coli response to uranyl exposure at low ph and associated protein regulations.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2014-01-01
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 coli cells 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 analyzed by 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.
url http://europepmc.org/articles/PMC3935937?pdf=render
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