Modification of thiol contents in poplars (Populus tremula x P. alba) overexpressing enzymes involved in glutathione synthesis.
Identifieur interne : 004985 ( Main/Exploration ); précédent : 004984; suivant : 004986Modification of thiol contents in poplars (Populus tremula x P. alba) overexpressing enzymes involved in glutathione synthesis.
Auteurs : A C Arisi [France] ; G. Noctor ; C H Foyer ; L. JouaninSource :
- Planta [ 0032-0935 ] ; 1997.
Descripteurs français
- KwdFr :
- Arbres (métabolisme), Cinétique (MeSH), Clonage moléculaire (MeSH), Escherichia coli (enzymologie), Glutamate-cysteine ligase (biosynthèse), Glutathion (métabolisme), Glutathione synthase (biosynthèse), Protéines recombinantes (biosynthèse), Thiols (métabolisme), Transcription génétique (MeSH), Végétaux génétiquement modifiés (MeSH).
- MESH :
- biosynthèse : Glutamate-cysteine ligase, Glutathione synthase, Protéines recombinantes.
- enzymologie : Escherichia coli.
- métabolisme : Arbres, Glutathion, Thiols.
- Cinétique, Clonage moléculaire, Transcription génétique, Végétaux génétiquement modifiés.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Escherichia coli (enzymology), Glutamate-Cysteine Ligase (biosynthesis), Glutathione (metabolism), Glutathione Synthase (biosynthesis), Kinetics (MeSH), Plants, Genetically Modified (MeSH), Recombinant Proteins (biosynthesis), Sulfhydryl Compounds (metabolism), Transcription, Genetic (MeSH), Trees (metabolism).
- MESH :
- chemical , biosynthesis : Glutamate-Cysteine Ligase, Glutathione Synthase, Recombinant Proteins.
- enzymology : Escherichia coli.
- chemical , metabolism : Glutathione, Sulfhydryl Compounds, Trees.
- Cloning, Molecular, Kinetics, Plants, Genetically Modified, Transcription, Genetic.
Abstract
The hybrid poplar (Populus tremula x P. alba) was transformed to express the Escherichia coli gene for gamma-glutamylcysteine synthetase (EC 6.3.2.2: gamma-ECS) in the cytosol. Four transformed lines of poplar were obtained. These were phenotypically indistinguishable from untransformed poplars. Three lines, ggs28 (Noctor et al. 1996, Plant Physiol 112: 1071-1078), ggs11 and ggs5 possessed high levels of bacterial gene transcripts. Line ggs17 had lower transcript levels. Antisera were prepared against bacterial gamma-ECS and bacterial glutathione synthetase (EC 6.3.2.3: GS). Using the antiserum prepared against the purified His-tagged E. coli gamma-ECS, lines ggs28, ggs11 and ggs5 were shown to possess abundant quantities of the bacterial protein, whereas ggs17 contained lower amounts. The antiserum prepared against the purified His-tagged E. coli GS was also effective in screening poplars transformed with the E. coli gene coding for this enzyme. Immunoblots of leaf extracts from poplars overexpressing GS using this antibody revealed two bands. The extractable foliar gamma-ECS activities of the gamma-ECS transformants were in quantitative agreement with the protein levels. Lines ggs28, ggs11 and ggs5 had approximately 30-fold higher gamma-ECS activity than untransformed poplars, whereas in ggs17 this activity was only augmented about 3-fold. The lines strongly overexpressing gamma-ECS, ggs28, ggs11 and ggs5, contained enhanced foliar levels of cysteine (up to 2-fold), gamma-glutamylcysteine (5- to 20-fold) and glutathione (2- to 4-fold). Foliar thiol contents in ggs17 were no different to those of untransformed plants.
DOI: 10.1007/s004250050202
PubMed: 9431683
Affiliations:
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Noctor</name></author><author><name sortKey="Foyer, C H" sort="Foyer, C H" uniqKey="Foyer C" first="C H" last="Foyer">C H Foyer</name></author><author><name sortKey="Jouanin, L" sort="Jouanin, L" uniqKey="Jouanin L" first="L" last="Jouanin">L. Jouanin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9431683</idno><idno type="pmid">9431683</idno><idno type="doi">10.1007/s004250050202</idno><idno type="wicri:Area/Main/Corpus">004A14</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004A14</idno><idno type="wicri:Area/Main/Curation">004A14</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004A14</idno><idno type="wicri:Area/Main/Exploration">004A14</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Modification of thiol contents in poplars (Populus tremula x P. alba) overexpressing enzymes involved in glutathione synthesis.</title><author><name sortKey="Arisi, A C" sort="Arisi, A C" uniqKey="Arisi A" first="A C" last="Arisi">A C Arisi</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Biologie Cellulaire, INRA, Versailles, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biologie Cellulaire, INRA, Versailles</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Versailles</settlement></placeName></affiliation></author><author><name sortKey="Noctor, G" sort="Noctor, G" uniqKey="Noctor G" first="G" last="Noctor">G. Noctor</name></author><author><name sortKey="Foyer, C H" sort="Foyer, C H" uniqKey="Foyer C" first="C H" last="Foyer">C H Foyer</name></author><author><name sortKey="Jouanin, L" sort="Jouanin, L" uniqKey="Jouanin L" first="L" last="Jouanin">L. Jouanin</name></author></analytic><series><title level="j">Planta</title><idno type="ISSN">0032-0935</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Escherichia coli (enzymology)</term><term>Glutamate-Cysteine Ligase (biosynthesis)</term><term>Glutathione (metabolism)</term><term>Glutathione Synthase (biosynthesis)</term><term>Kinetics (MeSH)</term><term>Plants, Genetically Modified (MeSH)</term><term>Recombinant Proteins (biosynthesis)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Transcription, Genetic (MeSH)</term><term>Trees (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arbres (métabolisme)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Glutamate-cysteine ligase (biosynthèse)</term><term>Glutathion (métabolisme)</term><term>Glutathione synthase (biosynthèse)</term><term>Protéines recombinantes (biosynthèse)</term><term>Thiols (métabolisme)</term><term>Transcription génétique (MeSH)</term><term>Végétaux génétiquement modifiés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glutamate-Cysteine Ligase</term><term>Glutathione Synthase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glutamate-cysteine ligase</term><term>Glutathione synthase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Sulfhydryl Compounds</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arbres</term><term>Glutathion</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Kinetics</term><term>Plants, Genetically Modified</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Transcription génétique</term><term>Végétaux génétiquement modifiés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The hybrid poplar (Populus tremula x P. alba) was transformed to express the Escherichia coli gene for gamma-glutamylcysteine synthetase (EC 6.3.2.2: gamma-ECS) in the cytosol. Four transformed lines of poplar were obtained. These were phenotypically indistinguishable from untransformed poplars. Three lines, ggs28 (Noctor et al. 1996, Plant Physiol 112: 1071-1078), ggs11 and ggs5 possessed high levels of bacterial gene transcripts. Line ggs17 had lower transcript levels. Antisera were prepared against bacterial gamma-ECS and bacterial glutathione synthetase (EC 6.3.2.3: GS). Using the antiserum prepared against the purified His-tagged E. coli gamma-ECS, lines ggs28, ggs11 and ggs5 were shown to possess abundant quantities of the bacterial protein, whereas ggs17 contained lower amounts. The antiserum prepared against the purified His-tagged E. coli GS was also effective in screening poplars transformed with the E. coli gene coding for this enzyme. Immunoblots of leaf extracts from poplars overexpressing GS using this antibody revealed two bands. The extractable foliar gamma-ECS activities of the gamma-ECS transformants were in quantitative agreement with the protein levels. Lines ggs28, ggs11 and ggs5 had approximately 30-fold higher gamma-ECS activity than untransformed poplars, whereas in ggs17 this activity was only augmented about 3-fold. The lines strongly overexpressing gamma-ECS, ggs28, ggs11 and ggs5, contained enhanced foliar levels of cysteine (up to 2-fold), gamma-glutamylcysteine (5- to 20-fold) and glutathione (2- to 4-fold). Foliar thiol contents in ggs17 were no different to those of untransformed plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9431683</PMID><DateCompleted><Year>1998</Year><Month>03</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>02</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0935</ISSN><JournalIssue CitedMedium="Print"><Volume>203</Volume><Issue>3</Issue><PubDate><Year>1997</Year></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Modification of thiol contents in poplars (Populus tremula x P. alba) overexpressing enzymes involved in glutathione synthesis.</ArticleTitle><Pagination><MedlinePgn>362-72</MedlinePgn></Pagination><Abstract><AbstractText>The hybrid poplar (Populus tremula x P. alba) was transformed to express the Escherichia coli gene for gamma-glutamylcysteine synthetase (EC 6.3.2.2: gamma-ECS) in the cytosol. Four transformed lines of poplar were obtained. These were phenotypically indistinguishable from untransformed poplars. Three lines, ggs28 (Noctor et al. 1996, Plant Physiol 112: 1071-1078), ggs11 and ggs5 possessed high levels of bacterial gene transcripts. Line ggs17 had lower transcript levels. Antisera were prepared against bacterial gamma-ECS and bacterial glutathione synthetase (EC 6.3.2.3: GS). Using the antiserum prepared against the purified His-tagged E. coli gamma-ECS, lines ggs28, ggs11 and ggs5 were shown to possess abundant quantities of the bacterial protein, whereas ggs17 contained lower amounts. The antiserum prepared against the purified His-tagged E. coli GS was also effective in screening poplars transformed with the E. coli gene coding for this enzyme. Immunoblots of leaf extracts from poplars overexpressing GS using this antibody revealed two bands. The extractable foliar gamma-ECS activities of the gamma-ECS transformants were in quantitative agreement with the protein levels. Lines ggs28, ggs11 and ggs5 had approximately 30-fold higher gamma-ECS activity than untransformed poplars, whereas in ggs17 this activity was only augmented about 3-fold. The lines strongly overexpressing gamma-ECS, ggs28, ggs11 and ggs5, contained enhanced foliar levels of cysteine (up to 2-fold), gamma-glutamylcysteine (5- to 20-fold) and glutathione (2- to 4-fold). Foliar thiol contents in ggs17 were no different to those of untransformed plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Arisi</LastName><ForeName>A C</ForeName><Initials>AC</Initials><AffiliationInfo><Affiliation>Laboratoire de Biologie Cellulaire, INRA, Versailles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Noctor</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Foyer</LastName><ForeName>C H</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Jouanin</LastName><ForeName>L</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.2.2</RegistryNumber><NameOfSubstance UI="D005721">Glutamate-Cysteine Ligase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.2.3</RegistryNumber><NameOfSubstance UI="D005981">Glutathione Synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>B</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005721" MajorTopicYN="N">Glutamate-Cysteine Ligase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005981" MajorTopicYN="N">Glutathione Synthase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>2</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9431683</ArticleId><ArticleId IdType="doi">10.1007/s004250050202</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Versailles</li></settlement></list><tree><noCountry><name sortKey="Foyer, C H" sort="Foyer, C H" uniqKey="Foyer C" first="C H" last="Foyer">C H Foyer</name><name sortKey="Jouanin, L" sort="Jouanin, L" uniqKey="Jouanin L" first="L" last="Jouanin">L. Jouanin</name><name sortKey="Noctor, G" sort="Noctor, G" uniqKey="Noctor G" first="G" last="Noctor">G. Noctor</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Arisi, A C" sort="Arisi, A C" uniqKey="Arisi A" first="A C" last="Arisi">A C Arisi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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