Glutamine synthetase activity in leaves of Zea mays L. as influenced by magnesium status.

CONCLUSIONS

The total capacity of the GS-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. Magnesium deficiency does not obligatorily lead to the decreased total protein concentrations in the leaves. Magnesium (Mg) is an integral component of the enzyme glutamine synthetase (GS), having both a structural and a catalytic role. Moreover, Mg is relevant for the post-translational regulation of the GS. Glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium (NH4 (+)) to glutamate to form glutamine and it is therefore crucial for plant growth and productivity. This study was conducted in order to test whether a severe Mg-deficiency impairs the total capacity of the GS-catalyzed synthesis of glutamine in maize leaves. Maize was grown hydroponically and the GS activity was analyzed dependent on different leaf developmental stages. Glutamine synthetase activity in vitro assays in combination with immune-dot blot analysis revealed that both the total activity and the abundance of glutamine synthetase was not impaired in the leaves of maize plants upon 54 days of severe Mg starvation. Additionally, it was shown that Mg deficiency does not obligatorily lead to decreased total protein concentrations in the leaves, as assayed by Bradford protein quantification. Moreover, Mg resupply to the roots or the leaves of Mg-deficient plants reversed the Mg-deficiency-induced accumulation of free amino acids in older leaves, which indicates impaired phloem loading. The results of our study reveal that the total GS-mediated primary or secondary assimilation of free NH4 (+) is not a limiting enzymatic reaction under Mg deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize.