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Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity

文献类型： 外文期刊

作者： Chao, Qing 1 ; Liu, Xiao-Yu 2 ; Mei, Ying-Chang 1 ; Gao, Zhi-Fang 1 ; Chen, Yi-Bo 1 ; Qian, Chun-Rong 3 ; Hao, Yu-Bo 3 ;

作者机构： 1.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing 100093, Peoples R China

2.Northeast Forestry Univ, State Key Lab Forest Genet & Tree Breeding, Harbin 150040, Peoples R China

3.Heilongjiang Acad Agr Sci, Inst Crop Cultivat & Farming, Harbin 150086, Peoples R China

关键词： Enzyme activity;Leaf sections;Light regulation;Maize;Phosphoenolpyruvate carboxykinase;Phosphorylation sites

期刊名称：PLANT MOLECULAR BIOLOGY （ 影响因子：4.076； 五年影响因子：4.89 ）

ISSN： 0167-4412

年卷期： 2014 年 85 卷 1-2 期

页码：

收录情况： SCI

摘要： Phosphoenolpyruvate carboxykinase (PEPCK)-the major decarboxylase in PEPCK-type C-4 plants-is also present in appreciable amounts in the bundle sheath cells of NADP-malic enzyme-type C-4 plants, such as maize (Zea mays), where it plays an apparent crucial role during photosynthesis (Wingler et al., in Plant Physiol 120(2):539-546, 1999; Furumoto et al., in Plant Mol Biol 41(3):301-311, 1999). Herein, we describe the use of mass spectrometry to demonstrate phosphorylation of maize PEPCK residues Ser55, Thr58, Thr59, and Thr120. Western blotting indicated that the extent of Ser55 phosphorylation dramatically increases in the leaves of maize seedlings when the seedlings are transferred from darkness to light, and decreases in the leaves of seedlings transferred from light to darkness. The effect of light on phosphorylation of this residue is opposite that of the effect of light on PEPCK activity, with the decarboxylase activity of PEPCK being less in illuminated leaves than in leaves left in the dark. This inverse relationship between PEPCK activity and the extent of phosphorylation suggests that the suppressive effect of light on PEPCK decarboxylation activity might be mediated by reversible phosphorylation of Ser55.

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