Phosphorylation by MPK6 A conserved transcriptional modification mediates nitrate reductase activation and NO production?
Phosphorylation by MPK6 A conserved transcriptional modification mediates nitrate reductase activation and NO production?
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DOI：
10.4161/psb.6.6.15308
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发表时间：
2011-01-01
影响因子：
2.9
通讯作者：
Song, Chun-Peng
中科院分区：
文献类型：
--
作者：
Wang, Pengcheng;Du, Yanyan;Song, Chun-Peng
硝酸还原酶是植物氮素同化的中心酶。在最近的工作中，我们发现MPK 6可以磷酸化拟南芥NIA 2铰链2区的第627位丝氨酸，这种磷酸化可能代表了植物需要过度减少硝酸盐时的快速激活机制。有趣的是，所有真核NR在其FAD结构域中都具有保守的对接序列，并且许多植物NR蛋白具有保守的MAPK磷酸化位点。这表明MAP激酶级联反应对NR蛋白的磷酸化在不同物种中可能是保守的。我们注意到MPK 6对S627残基的磷酸化对NO的产生有特殊的影响。虽然在高等植物中还没有发现哺乳动物NOS的同源性，但NR可能与哺乳动物NOS具有相似的调控机制。
Nitrate reductase is a central enzyme of nitrogen assimilation in plants. In a recent work, we have revealed MPK6 could phosphorylate Arabidopsis NIA2 at the serine 627 in hinge 2 region, this phosphorylation may represent a rapid activation mechnism when plant need excessive nitrate reduction. Interestingly, all eukaryotic NRs have conserved docking sequence in their FAD domains, and many plant NR proteins have the conserved MAPK phosphorylation site. Those indicated that phosphorylation of NR protein by MAP kinase cascade may be conserved in different species. We noticed that the phosphorylation of S627 residue by MPK6 have a specially influence on the NO generation. Although no homology of mammalian NOS has been identified in high plants, NR may still share a similar regulation mechanism with mammalian NOS.