PoplarV1, Main, Exploration, bibRecord, 002110

Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.

Identifieur interne : 002110 ( Main/Exploration ); précédent : 002109; suivant : 002111

Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.

Auteurs : Claudiu Niculaes [Belgique] ; Kris Morreel [Belgique] ; Hoon Kim [États-Unis] ; Fachuang Lu [États-Unis] ; Lauren S. Mckee [Suède] ; Bart Ivens [Belgique] ; Jurgen Haustraete [Belgique] ; Bartel Vanholme [Belgique] ; Riet De Rycke [Belgique] ; Magnus Hertzberg [Suède] ; Jorg Fromm [Allemagne] ; Vincent Bulone [Suède] ; Andrea Polle [Allemagne] ; John Ralph [États-Unis] ; Wout Boerjan [Belgique]

Source :

The Plant cell [ 1532-298X ] ; 2014.

RBID : pubmed:25238751

Descripteurs français

KwdFr :
- Acides aminés (métabolisme), Cystéine (métabolisme), Données de séquences moléculaires (MeSH), Dosages enzymatiques (MeSH), Immunotransfert (MeSH), Lignanes (biosynthèse), Lignanes (composition chimique), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Paroi cellulaire (métabolisme), Phénotype (MeSH), Populus (enzymologie), Reproductibilité des résultats (MeSH), Régulation négative (MeSH), Spectrométrie de masse (MeSH), Spectroscopie par résonance magnétique (MeSH), Spécificité du substrat (MeSH), Stress oxydatif (MeSH), Végétaux génétiquement modifiés (MeSH), Xylème (enzymologie).
MESH :
- biosynthèse : Lignanes.
- composition chimique : Lignanes, Oxidoreductases.
- enzymologie : Populus, Xylème.
- métabolisme : Acides aminés, Cystéine, Oxidoreductases, Paroi cellulaire.
- Données de séquences moléculaires, Dosages enzymatiques, Immunotransfert, Oxydoréduction, Phénotype, Reproductibilité des résultats, Régulation négative, Spectrométrie de masse, Spectroscopie par résonance magnétique, Spécificité du substrat, Stress oxydatif, Végétaux génétiquement modifiés.

English descriptors

KwdEn :
- Amino Acids (metabolism), Cell Wall (metabolism), Cysteine (metabolism), Down-Regulation (MeSH), Enzyme Assays (MeSH), Immunoblotting (MeSH), Lignans (biosynthesis), Lignans (chemistry), Magnetic Resonance Spectroscopy (MeSH), Mass Spectrometry (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Phenotype (MeSH), Plants, Genetically Modified (MeSH), Populus (enzymology), Reproducibility of Results (MeSH), Substrate Specificity (MeSH), Xylem (enzymology).
MESH :
- chemical , biosynthesis : Lignans.
- chemical , chemistry : Lignans, Oxidoreductases.
- chemical , metabolism : Amino Acids, Cysteine, Oxidoreductases.
- enzymology : Populus, Xylem.
- metabolism : Cell Wall.
- Down-Regulation, Enzyme Assays, Immunoblotting, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Sequence Data, Oxidation-Reduction, Oxidative Stress, Phenotype, Plants, Genetically Modified, Reproducibility of Results, Substrate Specificity.

Abstract

Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta.

DOI: 10.1105/tpc.114.125260
PubMed: 25238751
PubMed Central: PMC4213149

Affiliations:

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<placeName><region type="state">Wisconsin</region>
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<author><name sortKey="Boerjan, Wout" sort="Boerjan, Wout" uniqKey="Boerjan W" first="Wout" last="Boerjan">Wout Boerjan</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.</title>
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<country xml:lang="fr">Belgique</country>
<wicri:regionArea>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent</wicri:regionArea>
<orgName type="university">Université de Gand</orgName>
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<author><name sortKey="Morreel, Kris" sort="Morreel, Kris" uniqKey="Morreel K" first="Kris" last="Morreel">Kris Morreel</name>
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<country xml:lang="fr">Belgique</country>
<wicri:regionArea>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent</wicri:regionArea>
<orgName type="university">Université de Gand</orgName>
<placeName><settlement type="city">Gand</settlement>
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<author><name sortKey="Kim, Hoon" sort="Kim, Hoon" uniqKey="Kim H" first="Hoon" last="Kim">Hoon Kim</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and the U.S. Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Wisconsin</region>
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<author><name sortKey="Lu, Fachuang" sort="Lu, Fachuang" uniqKey="Lu F" first="Fachuang" last="Lu">Fachuang Lu</name>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Wisconsin</region>
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<author><name sortKey="Mckee, Lauren S" sort="Mckee, Lauren S" uniqKey="Mckee L" first="Lauren S" last="Mckee">Lauren S. Mckee</name>
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<country xml:lang="fr">Suède</country>
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<author><name sortKey="Ivens, Bart" sort="Ivens, Bart" uniqKey="Ivens B" first="Bart" last="Ivens">Bart Ivens</name>
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<author><name sortKey="Haustraete, Jurgen" sort="Haustraete, Jurgen" uniqKey="Haustraete J" first="Jurgen" last="Haustraete">Jurgen Haustraete</name>
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<author><name sortKey="Vanholme, Bartel" sort="Vanholme, Bartel" uniqKey="Vanholme B" first="Bartel" last="Vanholme">Bartel Vanholme</name>
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<country xml:lang="fr">Belgique</country>
<wicri:regionArea>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent</wicri:regionArea>
<orgName type="university">Université de Gand</orgName>
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<country xml:lang="fr">Belgique</country>
<wicri:regionArea>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent</wicri:regionArea>
<orgName type="university">Université de Gand</orgName>
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<author><name sortKey="Hertzberg, Magnus" sort="Hertzberg, Magnus" uniqKey="Hertzberg M" first="Magnus" last="Hertzberg">Magnus Hertzberg</name>
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<author><name sortKey="Fromm, Jorg" sort="Fromm, Jorg" uniqKey="Fromm J" first="Jorg" last="Fromm">Jorg Fromm</name>
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<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Zentrum für Holzwirtschaft, Universität Hamburg, D-21031 Hamburg</wicri:regionArea>
<wicri:noRegion>21031 Hamburg</wicri:noRegion>
<wicri:noRegion>21031 Hamburg</wicri:noRegion>
<wicri:noRegion>D-21031 Hamburg</wicri:noRegion>
</affiliation>
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<author><name sortKey="Bulone, Vincent" sort="Bulone, Vincent" uniqKey="Bulone V" first="Vincent" last="Bulone">Vincent Bulone</name>
<affiliation wicri:level="1"><nlm:affiliation>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden.</nlm:affiliation>
<country xml:lang="fr">Suède</country>
<wicri:regionArea>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm</wicri:regionArea>
<wicri:noRegion>106 91 Stockholm</wicri:noRegion>
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<author><name sortKey="Polle, Andrea" sort="Polle, Andrea" uniqKey="Polle A" first="Andrea" last="Polle">Andrea Polle</name>
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<author><name sortKey="Ralph, John" sort="Ralph, John" uniqKey="Ralph J" first="John" last="Ralph">John Ralph</name>
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<orgName type="university">Université de Gand</orgName>
<placeName><settlement type="city">Gand</settlement>
<region>Région flamande</region>
<region type="district" nuts="2">Province de Flandre-Orientale</region>
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<series><title level="j">The Plant cell</title>
<idno type="eISSN">1532-298X</idno>
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<term>Cell Wall (metabolism)</term>
<term>Cysteine (metabolism)</term>
<term>Down-Regulation (MeSH)</term>
<term>Enzyme Assays (MeSH)</term>
<term>Immunoblotting (MeSH)</term>
<term>Lignans (biosynthesis)</term>
<term>Lignans (chemistry)</term>
<term>Magnetic Resonance Spectroscopy (MeSH)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidative Stress (MeSH)</term>
<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phenotype (MeSH)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Populus (enzymology)</term>
<term>Reproducibility of Results (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Xylem (enzymology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term>
<term>Cystéine (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Dosages enzymatiques (MeSH)</term>
<term>Immunotransfert (MeSH)</term>
<term>Lignanes (biosynthèse)</term>
<term>Lignanes (composition chimique)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Paroi cellulaire (métabolisme)</term>
<term>Phénotype (MeSH)</term>
<term>Populus (enzymologie)</term>
<term>Reproductibilité des résultats (MeSH)</term>
<term>Régulation négative (MeSH)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Spectroscopie par résonance magnétique (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Stress oxydatif (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
<term>Xylème (enzymologie)</term>
</keywords>
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<term>Oxidoreductases</term>
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<term>Oxidoreductases</term>
</keywords>
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<term>Xylème</term>
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<term>Xylem</term>
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<term>Oxidoreductases</term>
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<term>Enzyme Assays</term>
<term>Immunoblotting</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
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<term>Plants, Genetically Modified</term>
<term>Reproducibility of Results</term>
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<term>Spectroscopie par résonance magnétique</term>
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<front><div type="abstract" xml:lang="en">Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta. </div>
</front>
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<DateCompleted><Year>2015</Year>
<Month>11</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-298X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>26</Volume>
<Issue>9</Issue>
<PubDate><Year>2014</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>The Plant cell</Title>
<ISOAbbreviation>Plant Cell</ISOAbbreviation>
</Journal>
<ArticleTitle>Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.</ArticleTitle>
<Pagination><MedlinePgn>3775-91</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1105/tpc.114.125260</ELocationID>
<Abstract><AbstractText>Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta. </AbstractText>
<CopyrightInformation>© 2014 American Society of Plant Biologists. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Niculaes</LastName>
<ForeName>Claudiu</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morreel</LastName>
<ForeName>Kris</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Hoon</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and the U.S. Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Fachuang</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and the U.S. Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McKee</LastName>
<ForeName>Lauren S</ForeName>
<Initials>LS</Initials>
<AffiliationInfo><Affiliation>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ivens</LastName>
<ForeName>Bart</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Haustraete</LastName>
<ForeName>Jurgen</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Protein Service Facility, Department for Molecular Biomedical Research, VIB, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vanholme</LastName>
<ForeName>Bartel</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rycke</LastName>
<ForeName>Riet De</ForeName>
<Initials>RD</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hertzberg</LastName>
<ForeName>Magnus</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>SweTree Technologies, SE-904 03 Umeå, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fromm</LastName>
<ForeName>Jorg</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Zentrum für Holzwirtschaft, Universität Hamburg, D-21031 Hamburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bulone</LastName>
<ForeName>Vincent</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Polle</LastName>
<ForeName>Andrea</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Forstbotanik und Baumphysiologie, Büsgen-Institut, Georg-August-Universität Göttingen, 37077 Göttingen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ralph</LastName>
<ForeName>John</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and the U.S. Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Boerjan</LastName>
<ForeName>Wout</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Department of Plant Systems Biology, VIB Institute, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium woboe@psb.vib-ugent.be.</Affiliation>
</AffiliationInfo>
</Author>
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<Language>eng</Language>
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Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.

Phenylcoumaran benzylic ether reductase prevents accumulation of compounds formed under oxidative conditions in poplar xylem.

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