tailieunhanh - báo cáo khoa học: "The glutamine synthetase gene family in Populus"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: The glutamine synthetase gene family in Populus | Castro-Rodriguez et al. BMC Plant Biology 2011 11 119 http 1471-2229 11 119 BMC Plant Biology RESEARCH ARTICLE Open Access The glutamine synthetase gene family in Populus 1a 1 1 1 2 Vanessa Castro-Rodriguez Angel García-Gutiérrez Javier Canales Concepcion Avila Edward G Kirby and Francisco M Cánovas1 Abstract Background Glutamine synthetase GS EC L-glutamate ammonia ligase ADP-forming is a key enzyme in ammonium assimilation and metabolism of higher plants. The current work was undertaken to develop a more comprehensive understanding of molecular and biochemical features of GS gene family in poplar and to characterize the developmental regulation of GS expression in various tissues and at various times during the poplar perennial growth. Results 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. Conclusions 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