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The glutamine synthetase gene family in Populus

DOI: 10.1186/1471-2229-11-119

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Abstract:

The GS gene family consists of 8 different genes exhibiting all structural and regulatory elements consistent with their roles as functional genes. Our results indicate that the family members are organized in 4 groups of duplicated genes, 3 of which code for cytosolic GS isoforms (GS1) and 1 which codes for the choroplastic GS isoform (GS2). Our analysis shows that Populus trichocarpa is the first plant species in which it was observed the complete GS family duplicated. Detailed expression analyses have revealed specific spatial and seasonal patterns of GS expression in poplar. These data provide insights into the metabolic function of GS isoforms in poplar and pave the way for future functional studies.Our data suggest that GS duplicates could have been retained in order to increase the amount of enzyme in a particular cell type. This possibility could contribute to the homeostasis of nitrogen metabolism in functions associated to changes in glutamine-derived metabolic products. The presence of duplicated GS genes in poplar could also contribute to diversification of the enzymatic properties for a particular GS isoform through the assembly of GS polypeptides into homo oligomeric and/or hetero oligomeric holoenzymes in specific cell types.Glutamine synthetase (GS; EC 6.3.1.2, L-glutamate: ammonia ligase ADP-forming) catalyzes the ATP-dependent addition of ammonium (NH4+) to the γ-carboxyl group of glutamate to produce glutamine and acts as the center for nitrogen flow in plants. Glutamate synthase (Fd-GOGAT, EC 1.4.7.1; NADH-GOGAT, EC 1.4.1.1) then catalyzes the conversion of glutamine and 2-oxoglutarate to produce two molecules of glutamate, one of which participates in further ammonium assimilation via GS while the other donates reduced nitrogen for all nitrogen-containing biomolecules [1]. The ammonium assimilated by GS in the production of glutamine can come from various sources, including direct uptake from the soil, reduction of nitrate and nitrite, photoresp

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