Nickel-induced changes in nitrogen metabolism in wheat shoots.
The influences of 50 and 100muM Ni on growth, tissue Ni accumulation, concentrations of nitrate, ammonium, glutamate, and proline as well as the activities of nitrate reductase (NR), nitrite reductase (NiR), glutamine synthetase (GS), glutamate synthase (GOGAT), glutamate dehydrogenase (GDH), alanine aminotransferase (AlaAT), and aspartate aminotransferase (AspAT) were examined in the shoots of wheat seedlings cv. Zyta. Exposure of the seedlings to Ni resulted in a rapid accumulation of this metal in the shoots, which was accompanied by significant reduction in fresh weight of these organs. Tissue nitrate content decreased in response to Ni stress, while ammonium concentration increased substantially. Glutamate concentration was slightly lowered up to the 4th day of the metal exposure. In contrast, proline content increased significantly, starting from the first day after Ni treatment. NR activity showed a decline of up to 40% below the control level after Ni application; however, its activation state remained unaltered. Heavy metal treatment also resulted in a marked decrease in NiR activity, which after 7d of exposure to 100muM Ni was almost 80% lower than in the control. GS activity in wheat shoots was not influenced by Ni application. Contrary to Fd-GOGAT exhibiting reduced activity in the shoots of Ni-treated wheat seedlings, NADH-GOGAT activity was considerably enhanced, exceeding the control value even by 165%. After 7d of exposure to Ni, both NADH-GDH and NAD-GDH activities in wheat shoots were markedly induced; however, NAD-GDH activity showed a significant decrease at the early stage of the experiment. Both AlaAT and AspAT glutamate-producing activities were considerably stimulated by Ni treatment. Our results suggest that induction of NADH-GOGAT, NADH-GDH, AlaAT, and AspAT activities may compensate for the reduced Fd-GOGAT activity and serve as an alternative means of glutamate synthesis in wheat shoots under Ni stress.
Gajewska
Ewa
E
Department of Plant Physiology and Biochemistry, University of Łódź, Banacha 12/16, 90-237 Łódź, Poland. ewagaj@biol.uni.lodz.pl
Skłodowska
Maria
M
D000410:Alanine Transaminase / Q000378:metabolism; D001219:Aspartate Aminotransferases / Q000378:metabolism; D018506:Gene Expression Regulation, Plant / Q000187:drug effects*; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D005970:Glutamate Synthase / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D018698:Glutamic Acid / Q000378:metabolism; D009532:Nickel / Q000494:pharmacology*; D050901:Nitrate Reductase / Q000378:metabolism; D009565:Nitrate Reductases / Q000378:metabolism; D009566:Nitrates / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism; D018520:Plant Shoots / Q000187:drug effects* / Q000378:metabolism*; D011392:Proline / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism; D014908:Triticum / Q000187:drug effects* / Q000378:metabolism*
D009566:Nitrates; D010940:Plant Proteins; D000644:Quaternary Ammonium Compounds; D018698:Glutamic Acid; D009532:Nickel; D011392:Proline; D005970:Glutamate Synthase; D005969:Glutamate Dehydrogenase; D009565:Nitrate Reductases; D050901:Nitrate Reductase; D001219:Aspartate Aminotransferases; D000410:Alanine Transaminase; D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen