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...
Main Authors: | , , , , , , , , , |
---|---|
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 |
id |
doaj-4a535c0d9e1543ccbe2fb7a39d3701d5 |
---|---|
record_format |
Article |
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 |
work_keys_str_mv |
AT arbiakhemiri escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT mariecarriere escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT nicolasbremond escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT mohamedaminebenmlouka escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT laurentcoquet escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT isabellellorens escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT virginiechapon escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT thierryjouenne escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT pascalcosette escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations AT catherineberthomieu escherichiacoliresponsetouranylexposureatlowphandassociatedproteinregulations |
_version_ |
1725916536451891200 |