title: Molecular and enzymatic analysis of ammonium assimilation in woody plants.
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.
authors.affiliation: Departamento de Biología Molecular y Bioquímica, Instituto Andaluz de Biotecnología, Unidad Asociada UMA-CSIC, Universidad de Málaga, E29071-Málaga, Spain.
authors.forename: María Fernanda
authors.initials: MF
authors.lastname: Suárez
authors.forename: Concepción
authors.initials: C
authors.lastname: Avila
authors.forename: Fernando
authors.initials: F
authors.lastname: Gallardo
authors.forename: Francisco R
authors.initials: FR
authors.lastname: Cantón
authors.forename: Angel
authors.initials: A
authors.lastname: García-Gutiérrez
authors.forename: M Gonzalo
authors.initials: MG
authors.lastname: Claros
authors.forename: Francisco M
authors.initials: FM
authors.lastname: Cánovas
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000235:genetics / Q000378:metabolism; D002244:Carbon / Q000378:metabolism; D032462:Cycadopsida / Q000201:enzymology / Q000235:genetics; D004798:Enzymes / Q000235:genetics* / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D005974:Glutamate-Ammonia Ligase / Q000235:genetics / Q000378:metabolism; D007521:Isocitrate Dehydrogenase / Q000235:genetics / Q000378:metabolism; D019684:Magnoliopsida / Q000201:enzymology / Q000235:genetics; D008928:Mitochondria / Q000201:enzymology; D009584:Nitrogen / Q000378:metabolism*; D010802:Phylogeny; D030821:Plants, Genetically Modified; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D014197:Trees / Q000201:enzymology / Q000235:genetics*
chemical_list: D004798:Enzymes; D000644:Quaternary Ammonium Compounds; D002244:Carbon; D007521:Isocitrate Dehydrogenase; D000594:Amino Acid Oxidoreductases; C042233:glutamate synthase (ferredoxin); D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen