Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana.
Identifieur interne : 002710 ( Main/Exploration ); précédent : 002709; suivant : 002711Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana.
Auteurs : Brigitte Poppenberger [Autriche] ; Franz Berthiller ; Doris Lucyshyn ; Tobias Sieberer ; Rainer Schuhmacher ; Rudolf Krska ; Karl Kuchler ; Josef Glössl ; Christian Luschnig ; Gerhard AdamSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- ADN complémentaire (métabolisme), ARN messager (métabolisme), Arabidopsis (enzymologie), Arabidopsis (microbiologie), Banque de gènes (MeSH), Carbone (composition chimique), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (métabolisme), Fusarium (métabolisme), Fusarium (pathogénicité), Glucosyltransferases (composition chimique), Glucosyltransferases (métabolisme), Glutathione transferase (métabolisme), Glycosylation (MeSH), Modèles chimiques (MeSH), Mycotoxines (métabolisme), Phénotype (MeSH), Protéines d'Arabidopsis (MeSH), RT-PCR (MeSH), Ribosomes (métabolisme), Régions promotrices (génétique) (MeSH), Similitude de séquences d'acides aminés (MeSH), Spectrométrie de masse (MeSH), Séquence d'acides aminés (MeSH), Transgènes (MeSH), Trichothécènes (métabolisme), Uridine diphosphate glucose (métabolisme), Vecteurs génétiques (MeSH).
- MESH :
- composition chimique : Carbone, Glucosyltransferases.
- enzymologie : Arabidopsis.
- microbiologie : Arabidopsis.
- métabolisme : ADN complémentaire, ARN messager, Escherichia coli, Fusarium, Glucosyltransferases, Glutathione transferase, Mycotoxines, Ribosomes, Trichothécènes, Uridine diphosphate glucose.
- pathogénicité : Fusarium.
- Banque de gènes, Clonage moléculaire, Conformation des protéines, Données de séquences moléculaires, Glycosylation, Modèles chimiques, Phénotype, Protéines d'Arabidopsis, RT-PCR, Régions promotrices (génétique), Similitude de séquences d'acides aminés, Spectrométrie de masse, Séquence d'acides aminés, Transgènes, Vecteurs génétiques.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (enzymology), Arabidopsis (microbiology), Arabidopsis Proteins (MeSH), Carbon (chemistry), Cloning, Molecular (MeSH), DNA, Complementary (metabolism), Escherichia coli (metabolism), Fusarium (metabolism), Fusarium (pathogenicity), Gene Library (MeSH), Genetic Vectors (MeSH), Glucosyltransferases (chemistry), Glucosyltransferases (metabolism), Glutathione Transferase (metabolism), Glycosylation (MeSH), Mass Spectrometry (MeSH), Models, Chemical (MeSH), Molecular Sequence Data (MeSH), Mycotoxins (metabolism), Phenotype (MeSH), Promoter Regions, Genetic (MeSH), Protein Conformation (MeSH), RNA, Messenger (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Ribosomes (metabolism), Sequence Homology, Amino Acid (MeSH), Transgenes (MeSH), Trichothecenes (metabolism), Uridine Diphosphate Glucose (metabolism).
- MESH :
- chemical , chemistry : Carbon, Glucosyltransferases.
- chemical , metabolism : DNA, Complementary, Glucosyltransferases, Glutathione Transferase, Mycotoxins, RNA, Messenger, Trichothecenes, Uridine Diphosphate Glucose.
- chemical : Arabidopsis Proteins.
- enzymology : Arabidopsis.
- metabolism : Escherichia coli, Fusarium, Ribosomes.
- microbiology : Arabidopsis.
- pathogenicity : Fusarium.
- Amino Acid Sequence, Cloning, Molecular, Gene Library, Genetic Vectors, Glycosylation, Mass Spectrometry, Models, Chemical, Molecular Sequence Data, Phenotype, Promoter Regions, Genetic, Protein Conformation, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Transgenes.
Abstract
Plant pathogenic fungi of the genus Fusarium cause agriculturally important diseases of small grain cereals and maize. Trichothecenes are a class of mycotoxins produced by different Fusarium species that inhibit eukaryotic protein biosynthesis and presumably interfere with the expression of genes induced during the defense response of the plants. One of its members, deoxynivalenol, most likely acts as a virulence factor during fungal pathogenesis and frequently accumulates in grain to levels posing a threat to human and animal health. We report the isolation and characterization of a gene from Arabidopsis thaliana encoding a UDP-glycosyltransferase that is able to detoxify deoxynivalenol. The enzyme, previously assigned the identifier UGT73C5, catalyzes the transfer of glucose from UDP-glucose to the hydroxyl group at carbon 3 of deoxynivalenol. Using a wheat germ extract-coupled transcription/translation system we have shown that this enzymatic reaction inactivates the mycotoxin. This deoxynivalenol-glucosyltransferase (DOGT1) was also found to detoxify the acetylated derivative 15-acetyl-deoxynivalenol, whereas no protective activity was observed against the structurally similar nivalenol. Expression of the glucosyltransferase is developmentally regulated and induced by deoxynivalenol as well as salicylic acid, ethylene, and jasmonic acid. Constitutive overexpression in Arabidopsis leads to enhanced tolerance against deoxynivalenol.
DOI: 10.1074/jbc.M307552200
PubMed: 12970342
Affiliations:
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Le document en format XML
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Complementary</term><term>Glucosyltransferases</term><term>Glutathione Transferase</term><term>Mycotoxins</term><term>RNA, Messenger</term><term>Trichothecenes</term><term>Uridine Diphosphate Glucose</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Arabidopsis Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbone</term><term>Glucosyltransferases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Fusarium</term><term>Ribosomes</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords 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Amino Acid</term><term>Transgenes</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de gènes</term><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glycosylation</term><term>Modèles chimiques</term><term>Phénotype</term><term>Protéines d'Arabidopsis</term><term>RT-PCR</term><term>Régions promotrices (génétique)</term><term>Similitude de séquences d'acides aminés</term><term>Spectrométrie de masse</term><term>Séquence d'acides aminés</term><term>Transgènes</term><term>Vecteurs génétiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant pathogenic fungi of the genus Fusarium cause agriculturally important diseases of small grain cereals and maize. Trichothecenes are a class of mycotoxins produced by different Fusarium species that inhibit eukaryotic protein biosynthesis and presumably interfere with the expression of genes induced during the defense response of the plants. One of its members, deoxynivalenol, most likely acts as a virulence factor during fungal pathogenesis and frequently accumulates in grain to levels posing a threat to human and animal health. We report the isolation and characterization of a gene from Arabidopsis thaliana encoding a UDP-glycosyltransferase that is able to detoxify deoxynivalenol. The enzyme, previously assigned the identifier UGT73C5, catalyzes the transfer of glucose from UDP-glucose to the hydroxyl group at carbon 3 of deoxynivalenol. Using a wheat germ extract-coupled transcription/translation system we have shown that this enzymatic reaction inactivates the mycotoxin. This deoxynivalenol-glucosyltransferase (DOGT1) was also found to detoxify the acetylated derivative 15-acetyl-deoxynivalenol, whereas no protective activity was observed against the structurally similar nivalenol. Expression of the glucosyltransferase is developmentally regulated and induced by deoxynivalenol as well as salicylic acid, ethylene, and jasmonic acid. Constitutive overexpression in Arabidopsis leads to enhanced tolerance against deoxynivalenol.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12970342</PMID><DateCompleted><Year>2004</Year><Month>01</Month><Day>12</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>278</Volume><Issue>48</Issue><PubDate><Year>2003</Year><Month>Nov</Month><Day>28</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana.</ArticleTitle><Pagination><MedlinePgn>47905-14</MedlinePgn></Pagination><Abstract><AbstractText>Plant pathogenic fungi of the genus Fusarium cause agriculturally important diseases of small grain cereals and maize. Trichothecenes are a class of mycotoxins produced by different Fusarium species that inhibit eukaryotic protein biosynthesis and presumably interfere with the expression of genes induced during the defense response of the plants. One of its members, deoxynivalenol, most likely acts as a virulence factor during fungal pathogenesis and frequently accumulates in grain to levels posing a threat to human and animal health. We report the isolation and characterization of a gene from Arabidopsis thaliana encoding a UDP-glycosyltransferase that is able to detoxify deoxynivalenol. The enzyme, previously assigned the identifier UGT73C5, catalyzes the transfer of glucose from UDP-glucose to the hydroxyl group at carbon 3 of deoxynivalenol. Using a wheat germ extract-coupled transcription/translation system we have shown that this enzymatic reaction inactivates the mycotoxin. This deoxynivalenol-glucosyltransferase (DOGT1) was also found to detoxify the acetylated derivative 15-acetyl-deoxynivalenol, whereas no protective activity was observed against the structurally similar nivalenol. Expression of the glucosyltransferase is developmentally regulated and induced by deoxynivalenol as well as salicylic acid, ethylene, and jasmonic acid. Constitutive overexpression in Arabidopsis leads to enhanced tolerance against deoxynivalenol.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Poppenberger</LastName><ForeName>Brigitte</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Center of Applied Genetics, BOKU - University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berthiller</LastName><ForeName>Franz</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Lucyshyn</LastName><ForeName>Doris</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Sieberer</LastName><ForeName>Tobias</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Schuhmacher</LastName><ForeName>Rainer</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Krska</LastName><ForeName>Rudolf</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Kuchler</LastName><ForeName>Karl</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Glössl</LastName><ForeName>Josef</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Luschnig</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Adam</LastName><ForeName>Gerhard</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>09</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009183">Mycotoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014255">Trichothecenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-44-0</RegistryNumber><NameOfSubstance UI="D002244">Carbon</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="C480166">Dogt1 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="D005964">Glucosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>JT37HYP23V</RegistryNumber><NameOfSubstance UI="C007262">deoxynivalenol</NameOfSubstance></Chemical><Chemical><RegistryNumber>V50K1D7P4Y</RegistryNumber><NameOfSubstance UI="D014532">Uridine Diphosphate Glucose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002244" MajorTopicYN="N">Carbon</DescriptorName><QualifierName UI="Q000737" 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PubStatus="entrez"><Year>2003</Year><Month>9</Month><Day>13</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12970342</ArticleId><ArticleId IdType="doi">10.1074/jbc.M307552200</ArticleId><ArticleId IdType="pii">M307552200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Autriche</li></country></list><tree><noCountry><name sortKey="Adam, Gerhard" sort="Adam, Gerhard" uniqKey="Adam G" first="Gerhard" last="Adam">Gerhard Adam</name><name sortKey="Berthiller, Franz" sort="Berthiller, Franz" uniqKey="Berthiller F" first="Franz" last="Berthiller">Franz Berthiller</name><name sortKey="Glossl, Josef" sort="Glossl, Josef" uniqKey="Glossl J" first="Josef" last="Glössl">Josef Glössl</name><name sortKey="Krska, Rudolf" sort="Krska, Rudolf" uniqKey="Krska R" first="Rudolf" last="Krska">Rudolf Krska</name><name sortKey="Kuchler, Karl" sort="Kuchler, Karl" uniqKey="Kuchler K" first="Karl" last="Kuchler">Karl Kuchler</name><name sortKey="Lucyshyn, Doris" sort="Lucyshyn, Doris" uniqKey="Lucyshyn D" first="Doris" last="Lucyshyn">Doris Lucyshyn</name><name sortKey="Luschnig, Christian" sort="Luschnig, Christian" uniqKey="Luschnig C" first="Christian" last="Luschnig">Christian Luschnig</name><name sortKey="Schuhmacher, Rainer" sort="Schuhmacher, Rainer" uniqKey="Schuhmacher R" first="Rainer" last="Schuhmacher">Rainer Schuhmacher</name><name sortKey="Sieberer, Tobias" sort="Sieberer, Tobias" uniqKey="Sieberer T" first="Tobias" last="Sieberer">Tobias Sieberer</name></noCountry><country name="Autriche"><noRegion><name sortKey="Poppenberger, Brigitte" sort="Poppenberger, Brigitte" uniqKey="Poppenberger B" first="Brigitte" last="Poppenberger">Brigitte Poppenberger</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= DetoxFungiV1
|flux= Main
|étape= Exploration
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|clé= pubmed:12970342
|texte= Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana.
}}
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