Molecular and enzymatic analysis of ammonium assimilation in woody plants.
Identifieur interne : 004557 ( Main/Exploration ); précédent : 004556; suivant : 004558Molecular and enzymatic analysis of ammonium assimilation in woody plants.
Auteurs : María Fernanda Suárez [Espagne] ; Concepci N Avila ; Fernando Gallardo ; Francisco R. Cant N ; Angel García-Gutiérrez ; M Gonzalo Claros ; Francisco M. CánovasSource :
- Journal of experimental botany [ 0022-0957 ] ; 2002.
Descripteurs français
- KwdFr :
- Amino-acid oxidoreductases (génétique), Amino-acid oxidoreductases (métabolisme), Arbres (enzymologie), Arbres (génétique), Azote (métabolisme), Carbone (métabolisme), Composés d'ammonium quaternaire (métabolisme), Cycadopsida (enzymologie), Cycadopsida (génétique), Enzymes (génétique), Enzymes (métabolisme), Glutamate-ammonia ligase (génétique), Glutamate-ammonia ligase (métabolisme), Isocitrate dehydrogenases (génétique), Isocitrate dehydrogenases (métabolisme), Magnoliopsida (enzymologie), Magnoliopsida (génétique), Mitochondries (enzymologie), Phylogenèse (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Végétaux génétiquement modifiés (MeSH).
- MESH :
- enzymologie : Arbres, Cycadopsida, Magnoliopsida, Mitochondries.
- génétique : Amino-acid oxidoreductases, Arbres, Cycadopsida, Enzymes, Glutamate-ammonia ligase, Isocitrate dehydrogenases, Magnoliopsida.
- métabolisme : Amino-acid oxidoreductases, Azote, Carbone, Composés d'ammonium quaternaire, Enzymes, Glutamate-ammonia ligase, Isocitrate dehydrogenases.
- Phylogenèse, Régulation de l'expression des gènes végétaux, Végétaux génétiquement modifiés.
English descriptors
- KwdEn :
- Amino Acid Oxidoreductases (genetics), Amino Acid Oxidoreductases (metabolism), Carbon (metabolism), Cycadopsida (enzymology), Cycadopsida (genetics), Enzymes (genetics), Enzymes (metabolism), Gene Expression Regulation, Plant (MeSH), Glutamate-Ammonia Ligase (genetics), Glutamate-Ammonia Ligase (metabolism), Isocitrate Dehydrogenase (genetics), Isocitrate Dehydrogenase (metabolism), Magnoliopsida (enzymology), Magnoliopsida (genetics), Mitochondria (enzymology), Nitrogen (metabolism), Phylogeny (MeSH), Plants, Genetically Modified (MeSH), Quaternary Ammonium Compounds (metabolism), Trees (enzymology), Trees (genetics).
- MESH :
- chemical , genetics : Amino Acid Oxidoreductases, Enzymes, Glutamate-Ammonia Ligase, Isocitrate Dehydrogenase.
- chemical , metabolism : Amino Acid Oxidoreductases, Carbon, Enzymes, Glutamate-Ammonia Ligase, Isocitrate Dehydrogenase, Nitrogen, Quaternary Ammonium Compounds.
- enzymology : Cycadopsida, Magnoliopsida, Mitochondria, Trees.
- genetics : Cycadopsida, Magnoliopsida, Trees.
- Gene Expression Regulation, Plant, Phylogeny, Plants, Genetically Modified.
Abstract
Ammonium is assimilated into amino acids through the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) enzymes. This metabolic pathway is driven by energy, reducing power and requires the net supply of 2-oxoglutarate that can be provided by the reaction catalysed by isocitrate dehydrogenase (IDH). Most studies on the biochemistry and molecular biology of N-assimilating enzymes have been carried out on annual plant species and the available information on woody models is far more limited. This is in spite of their economic and ecological importance and the fact that nitrogen is a common limiting factor for tree growth. GS, GOGAT and IDH enzymes have been purified from several woody species and their kinetic and molecular properties determined. A number of cDNA clones have also been isolated and characterized. Although the enzymes are remarkably well conserved along the evolutionary scale, major differences have been found in their compartmentation within the cell between angiosperms and conifers, suggesting possible adaptations to specific functional roles. The analysis of the gene expression patterns in a variety of biological situations such as changes in N nutrition, development, biotic or abiotic stresses and senescence, suggest that cytosolic GS plays a central and pivotal role in ammonium assimilation and metabolism in woody plants. The modification of N assimilation efficiency has been recently approached in trees by overexpression of a cytosolic pine GS in poplar. The results obtained, suggest that an increase in cytosolic GS might lead to a global effect on the synthesis of nitrogenous compounds in the leaves, with enhanced vegetative growth of transgenic trees. All these data suggest that manipulation of cytosolic GS may have consequences for plant growth and biomass production.
DOI: 10.1093/jexbot/53.370.891
PubMed: 11912232
Affiliations:
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This metabolic pathway is driven by energy, reducing power and requires the net supply of 2-oxoglutarate that can be provided by the reaction catalysed by isocitrate dehydrogenase (IDH). Most studies on the biochemistry and molecular biology of N-assimilating enzymes have been carried out on annual plant species and the available information on woody models is far more limited. This is in spite of their economic and ecological importance and the fact that nitrogen is a common limiting factor for tree growth. GS, GOGAT and IDH enzymes have been purified from several woody species and their kinetic and molecular properties determined. A number of cDNA clones have also been isolated and characterized. Although the enzymes are remarkably well conserved along the evolutionary scale, major differences have been found in their compartmentation within the cell between angiosperms and conifers, suggesting possible adaptations to specific functional roles. The analysis of the gene expression patterns in a variety of biological situations such as changes in N nutrition, development, biotic or abiotic stresses and senescence, suggest that cytosolic GS plays a central and pivotal role in ammonium assimilation and metabolism in woody plants. The modification of N assimilation efficiency has been recently approached in trees by overexpression of a cytosolic pine GS in poplar. The results obtained, suggest that an increase in cytosolic GS might lead to a global effect on the synthesis of nitrogenous compounds in the leaves, with enhanced vegetative growth of transgenic trees. All these data suggest that manipulation of cytosolic GS may have consequences for plant growth and biomass production.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11912232</PMID><DateCompleted><Year>2002</Year><Month>07</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-0957</ISSN><JournalIssue CitedMedium="Print"><Volume>53</Volume><Issue>370</Issue><PubDate><Year>2002</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of experimental botany</Title><ISOAbbreviation>J Exp Bot</ISOAbbreviation></Journal><ArticleTitle>Molecular and enzymatic analysis of ammonium assimilation in woody plants.</ArticleTitle><Pagination><MedlinePgn>891-904</MedlinePgn></Pagination><Abstract><AbstractText>Ammonium is assimilated into amino acids through the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) enzymes. This metabolic pathway is driven by energy, reducing power and requires the net supply of 2-oxoglutarate that can be provided by the reaction catalysed by isocitrate dehydrogenase (IDH). Most studies on the biochemistry and molecular biology of N-assimilating enzymes have been carried out on annual plant species and the available information on woody models is far more limited. This is in spite of their economic and ecological importance and the fact that nitrogen is a common limiting factor for tree growth. GS, GOGAT and IDH enzymes have been purified from several woody species and their kinetic and molecular properties determined. A number of cDNA clones have also been isolated and characterized. Although the enzymes are remarkably well conserved along the evolutionary scale, major differences have been found in their compartmentation within the cell between angiosperms and conifers, suggesting possible adaptations to specific functional roles. The analysis of the gene expression patterns in a variety of biological situations such as changes in N nutrition, development, biotic or abiotic stresses and senescence, suggest that cytosolic GS plays a central and pivotal role in ammonium assimilation and metabolism in woody plants. The modification of N assimilation efficiency has been recently approached in trees by overexpression of a cytosolic pine GS in poplar. The results obtained, suggest that an increase in cytosolic GS might lead to a global effect on the synthesis of nitrogenous compounds in the leaves, with enhanced vegetative growth of transgenic trees. All these data suggest that manipulation of cytosolic GS may have consequences for plant growth and biomass production.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Suárez</LastName><ForeName>María Fernanda</ForeName><Initials>MF</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Instituto Andaluz de Biotecnología, Unidad Asociada UMA-CSIC, Universidad de Málaga, E29071-Málaga, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Avila</LastName><ForeName>Concepción</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Gallardo</LastName><ForeName>Fernando</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Cantón</LastName><ForeName>Francisco R</ForeName><Initials>FR</Initials></Author><Author ValidYN="Y"><LastName>García-Gutiérrez</LastName><ForeName>Angel</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Claros</LastName><ForeName>M Gonzalo</ForeName><Initials>MG</Initials></Author><Author ValidYN="Y"><LastName>Cánovas</LastName><ForeName>Francisco M</ForeName><Initials>FM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Exp Bot</MedlineTA><NlmUniqueID>9882906</NlmUniqueID><ISSNLinking>0022-0957</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004798">Enzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000644">Quaternary Ammonium Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-44-0</RegistryNumber><NameOfSubstance UI="D002244">Carbon</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.41</RegistryNumber><NameOfSubstance UI="D007521">Isocitrate Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.4.-</RegistryNumber><NameOfSubstance UI="D000594">Amino Acid Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.4.7.1</RegistryNumber><NameOfSubstance UI="C042233">glutamate synthase (ferredoxin)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.1.2</RegistryNumber><NameOfSubstance UI="D005974">Glutamate-Ammonia Ligase</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000594" MajorTopicYN="N">Amino Acid Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002244" MajorTopicYN="N">Carbon</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032462" MajorTopicYN="N">Cycadopsida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004798" MajorTopicYN="N">Enzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005974" MajorTopicYN="N">Glutamate-Ammonia Ligase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007521" MajorTopicYN="N">Isocitrate Dehydrogenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019684" MajorTopicYN="N">Magnoliopsida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000644" MajorTopicYN="N">Quaternary Ammonium Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>77</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>3</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>7</Month><Day>20</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>3</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11912232</ArticleId><ArticleId IdType="doi">10.1093/jexbot/53.370.891</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Andalousie</li></region><settlement><li>Malaga</li></settlement><orgName><li>Université de Malaga</li></orgName></list><tree><noCountry><name sortKey="Avila, Concepci N" sort="Avila, Concepci N" uniqKey="Avila C" first="Concepci N" last="Avila">Concepci N Avila</name><name sortKey="Canovas, Francisco M" sort="Canovas, Francisco M" uniqKey="Canovas F" first="Francisco M" last="Cánovas">Francisco M. Cánovas</name><name sortKey="Cant N, Francisco R" sort="Cant N, Francisco R" uniqKey="Cant N F" first="Francisco R" last="Cant N">Francisco R. Cant N</name><name sortKey="Claros, M Gonzalo" sort="Claros, M Gonzalo" uniqKey="Claros M" first="M Gonzalo" last="Claros">M Gonzalo Claros</name><name sortKey="Gallardo, Fernando" sort="Gallardo, Fernando" uniqKey="Gallardo F" first="Fernando" last="Gallardo">Fernando Gallardo</name><name sortKey="Garcia Gutierrez, Angel" sort="Garcia Gutierrez, Angel" uniqKey="Garcia Gutierrez A" first="Angel" last="García-Gutiérrez">Angel García-Gutiérrez</name></noCountry><country name="Espagne"><region name="Andalousie"><name sortKey="Suarez, Maria Fernanda" sort="Suarez, Maria Fernanda" uniqKey="Suarez M" first="María Fernanda" last="Suárez">María Fernanda Suárez</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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