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How do three cytosolic glutamine synthetase isozymes of wheat perform N assimilation and translocation?

By Yihao Wei, Xiaochun Wang, Zhiyong Zhang, Shuping Xiong, Yiming Zhang, Lulu Wang, Xiaodan Meng, Jie Zhang, Xinming Ma

Posted 14 Aug 2019
bioRxiv DOI: 10.1101/733857

To understand how the three cytosolic glutamine synthetase (GS1) isozymes of wheat (Triticum aestivum L., TaGS1) perform nitrogen assimilation and translocation, we studied the kinetic properties of TaGS1 isozymes, the effects of nitrogen on the expression and localization of TaGS1 isozymes with specific antibodies, and the nitrogen metabolism. The results showed TaGS1;1, the dominant TaGS1 isozyme, had a high affinity for substrates, and was widely localized in the mesophyll cells, root pericycle and root tip meristematic zone, suggesting it was the primary isozyme for N assimilation. TaGS1;2, with a high affinity for Glu, was activated by Gln, and was mainly localized in the around vascular tissues, indicating that TaGS1;2 catalyzed Gln synthesis in low Glu concentration, then the Gln returned to activate TaGS1;2, which may lead to the rapid accumulation of Gln around the vascular tissues. TaGS1;3 had low affinity for substrates but the highest Vmax among TaGS1, was mainly localized in the root tip meristematic zone; exogenous NH4+ could promote TaGS1;3 expressing, indicating that TaGS1;3 could rapidly assimilate NH4+ to relieve NH4+ toxicity. In conclusion, TaGS1;1, TaGS1;2 and TaGS1;3 have different role in N assimilation, Gln translocation and relieving ammonium toxicity, respectively, and synergistically perform nitrogen assimilation and translocation.

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