Plant-based FRET biosensor discriminates environmental zinc levels.
Identifieur interne : 002953 ( Main/Exploration ); précédent : 002952; suivant : 002954Plant-based FRET biosensor discriminates environmental zinc levels.
Auteurs : Joshua P. Adams [États-Unis] ; Ardeshir Adeli ; Chuan-Yu Hsu ; Richard L. Harkess ; Grier P. Page ; Claude W. Depamphilis ; Emily B. Schultz ; Cetin YuceerSource :
- Plant biotechnology journal [ 1467-7652 ] ; 2012.
Descripteurs français
- KwdFr :
- Arabidopsis (composition chimique), Arabidopsis (génétique), Arabidopsis (métabolisme), Microscopie de fluorescence (MeSH), Polluants du sol (analyse), Polluants du sol (pharmacocinétique), Populus (composition chimique), Populus (génétique), Populus (métabolisme), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines luminescentes (composition chimique), Protéines luminescentes (génétique), Protéines luminescentes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Surveillance de l'environnement (méthodes), Techniques de biocapteur (méthodes), Transfert d'énergie par résonance de fluorescence (méthodes), Transporteurs de cations (composition chimique), Transporteurs de cations (génétique), Transporteurs de cations (métabolisme), Zinc (analyse), Zinc (pharmacocinétique).
- MESH :
- analyse : Polluants du sol, Zinc.
- composition chimique : Arabidopsis, Populus, Protéines de fusion recombinantes, Protéines luminescentes, Protéines végétales, Transporteurs de cations.
- génétique : Arabidopsis, Populus, Protéines de fusion recombinantes, Protéines luminescentes, Protéines végétales, Transporteurs de cations.
- métabolisme : Arabidopsis, Populus, Protéines de fusion recombinantes, Protéines luminescentes, Protéines végétales, Transporteurs de cations.
- méthodes : Surveillance de l'environnement, Techniques de biocapteur, Transfert d'énergie par résonance de fluorescence.
- pharmacocinétique : Polluants du sol, Zinc.
- Microscopie de fluorescence.
English descriptors
- KwdEn :
- Arabidopsis (chemistry), Arabidopsis (genetics), Arabidopsis (metabolism), Biosensing Techniques (methods), Cation Transport Proteins (chemistry), Cation Transport Proteins (genetics), Cation Transport Proteins (metabolism), Environmental Monitoring (methods), Fluorescence Resonance Energy Transfer (methods), Luminescent Proteins (chemistry), Luminescent Proteins (genetics), Luminescent Proteins (metabolism), Microscopy, Fluorescence (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (chemistry), Populus (genetics), Populus (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Soil Pollutants (analysis), Soil Pollutants (pharmacokinetics), Zinc (analysis), Zinc (pharmacokinetics).
- MESH :
- chemical , analysis : Soil Pollutants, Zinc.
- chemical , chemistry : Cation Transport Proteins, Luminescent Proteins, Plant Proteins, Recombinant Fusion Proteins.
- chemistry : Arabidopsis, Populus.
- genetics : Arabidopsis, Cation Transport Proteins, Luminescent Proteins, Plant Proteins, Populus, Recombinant Fusion Proteins.
- metabolism : Arabidopsis, Cation Transport Proteins, Luminescent Proteins, Plant Proteins, Populus, Recombinant Fusion Proteins.
- methods : Biosensing Techniques, Environmental Monitoring, Fluorescence Resonance Energy Transfer.
- chemical , pharmacokinetics : Soil Pollutants, Zinc.
- Microscopy, Fluorescence.
Abstract
Heavy metal accumulation in the environment poses great risks to flora and fauna. However, monitoring sites prone to accumulation poses scale and economic challenges. In this study, we present and test a method for monitoring these sites using fluorescent resonance energy transfer (FRET) change in response to zinc (Zn) accumulation in plants as a proxy for environmental health. We modified a plant Zn transport protein by adding flanking fluorescent proteins (FPs) and deploying the construct into two different species. In Arabidopsis thaliana, FRET was monitored by a confocal microscope and had a 1.4-fold increase in intensity as the metal concentration increased. This led to a 16.7% overall error-rate when discriminating between a control (1μm Zn) and high (10mm Zn) treatment after 96h. The second host plant (Populus tremula×Populu salba) also had greater FRET values (1.3-fold increase) when exposed to the higher concentration of Zn, while overall error-rates were greater at 22.4%. These results indicate that as plants accumulate Zn, protein conformational changes occur in response to Zn causing differing interaction between FPs. This results in greater FRET values when exposed to greater amounts of Zn and monitored with appropriate light sources and filters. We also demonstrate how this construct can be moved into different host plants effectively including one tree species. This chimeric protein potentially offers a method for monitoring large areas of land for Zn accumulation, is transferable among species, and could be modified to monitor other specific heavy metals that pose environmental risks.
DOI: 10.1111/j.1467-7652.2011.00656.x
PubMed: 21910820
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<front><div type="abstract" xml:lang="en">Heavy metal accumulation in the environment poses great risks to flora and fauna. However, monitoring sites prone to accumulation poses scale and economic challenges. In this study, we present and test a method for monitoring these sites using fluorescent resonance energy transfer (FRET) change in response to zinc (Zn) accumulation in plants as a proxy for environmental health. We modified a plant Zn transport protein by adding flanking fluorescent proteins (FPs) and deploying the construct into two different species. In Arabidopsis thaliana, FRET was monitored by a confocal microscope and had a 1.4-fold increase in intensity as the metal concentration increased. This led to a 16.7% overall error-rate when discriminating between a control (1μm Zn) and high (10mm Zn) treatment after 96h. The second host plant (Populus tremula×Populu salba) also had greater FRET values (1.3-fold increase) when exposed to the higher concentration of Zn, while overall error-rates were greater at 22.4%. These results indicate that as plants accumulate Zn, protein conformational changes occur in response to Zn causing differing interaction between FPs. This results in greater FRET values when exposed to greater amounts of Zn and monitored with appropriate light sources and filters. We also demonstrate how this construct can be moved into different host plants effectively including one tree species. This chimeric protein potentially offers a method for monitoring large areas of land for Zn accumulation, is transferable among species, and could be modified to monitor other specific heavy metals that pose environmental risks.</div>
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<Month>07</Month>
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<Title>Plant biotechnology journal</Title>
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<ArticleTitle>Plant-based FRET biosensor discriminates environmental zinc levels.</ArticleTitle>
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<Abstract><AbstractText>Heavy metal accumulation in the environment poses great risks to flora and fauna. However, monitoring sites prone to accumulation poses scale and economic challenges. In this study, we present and test a method for monitoring these sites using fluorescent resonance energy transfer (FRET) change in response to zinc (Zn) accumulation in plants as a proxy for environmental health. We modified a plant Zn transport protein by adding flanking fluorescent proteins (FPs) and deploying the construct into two different species. In Arabidopsis thaliana, FRET was monitored by a confocal microscope and had a 1.4-fold increase in intensity as the metal concentration increased. This led to a 16.7% overall error-rate when discriminating between a control (1μm Zn) and high (10mm Zn) treatment after 96h. The second host plant (Populus tremula×Populu salba) also had greater FRET values (1.3-fold increase) when exposed to the higher concentration of Zn, while overall error-rates were greater at 22.4%. These results indicate that as plants accumulate Zn, protein conformational changes occur in response to Zn causing differing interaction between FPs. This results in greater FRET values when exposed to greater amounts of Zn and monitored with appropriate light sources and filters. We also demonstrate how this construct can be moved into different host plants effectively including one tree species. This chimeric protein potentially offers a method for monitoring large areas of land for Zn accumulation, is transferable among species, and could be modified to monitor other specific heavy metals that pose environmental risks.</AbstractText>
<CopyrightInformation>© 2011 The Authors. Plant Biotechnology Journal © 2011 Society for Experimental Biology, Association of Applied Biologists and Blackwell Publishing Ltd.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Adams</LastName>
<ForeName>Joshua P</ForeName>
<Initials>JP</Initials>
<AffiliationInfo><Affiliation>School of Forest Resources, University of Arkansas at Monticello, Monticello, AR, USA. adamsj@uamont.edu</Affiliation>
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<ForeName>Ardeshir</ForeName>
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<ForeName>Chuan-Yu</ForeName>
<Initials>CY</Initials>
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<Author ValidYN="Y"><LastName>Harkess</LastName>
<ForeName>Richard L</ForeName>
<Initials>RL</Initials>
</Author>
<Author ValidYN="Y"><LastName>Page</LastName>
<ForeName>Grier P</ForeName>
<Initials>GP</Initials>
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<Author ValidYN="Y"><LastName>Depamphilis</LastName>
<ForeName>Claude W</ForeName>
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<Author ValidYN="Y"><LastName>Schultz</LastName>
<ForeName>Emily B</ForeName>
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<Author ValidYN="Y"><LastName>Yuceer</LastName>
<ForeName>Cetin</ForeName>
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<PubMedPubDate PubStatus="medline"><Year>2012</Year>
<Month>7</Month>
<Day>7</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">21910820</ArticleId>
<ArticleId IdType="doi">10.1111/j.1467-7652.2011.00656.x</ArticleId>
</ArticleIdList>
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<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Arkansas</li>
</region>
</list>
<tree><noCountry><name sortKey="Adeli, Ardeshir" sort="Adeli, Ardeshir" uniqKey="Adeli A" first="Ardeshir" last="Adeli">Ardeshir Adeli</name>
<name sortKey="Depamphilis, Claude W" sort="Depamphilis, Claude W" uniqKey="Depamphilis C" first="Claude W" last="Depamphilis">Claude W. Depamphilis</name>
<name sortKey="Harkess, Richard L" sort="Harkess, Richard L" uniqKey="Harkess R" first="Richard L" last="Harkess">Richard L. Harkess</name>
<name sortKey="Hsu, Chuan Yu" sort="Hsu, Chuan Yu" uniqKey="Hsu C" first="Chuan-Yu" last="Hsu">Chuan-Yu Hsu</name>
<name sortKey="Page, Grier P" sort="Page, Grier P" uniqKey="Page G" first="Grier P" last="Page">Grier P. Page</name>
<name sortKey="Schultz, Emily B" sort="Schultz, Emily B" uniqKey="Schultz E" first="Emily B" last="Schultz">Emily B. Schultz</name>
<name sortKey="Yuceer, Cetin" sort="Yuceer, Cetin" uniqKey="Yuceer C" first="Cetin" last="Yuceer">Cetin Yuceer</name>
</noCountry>
<country name="États-Unis"><region name="Arkansas"><name sortKey="Adams, Joshua P" sort="Adams, Joshua P" uniqKey="Adams J" first="Joshua P" last="Adams">Joshua P. Adams</name>
</region>
</country>
</tree>
</affiliations>
</record>
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