Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity
文献类型：期刊论文
| 作者 | Chao, Qing; Liu, Xiao-Yu; Mei, Ying-Chang; Gao, Zhi-Fang; Chen, Yi-Bo; Qian, Chun-Rong; Hao, Yu-Bo; Wang, Bai-Chen |
| 刊名 | PLANT MOLECULAR BIOLOGY
 |
| 出版日期 | 2014 |
| 卷号 | 85期号:1-2页码:95-105 |
| 关键词 | Enzyme activity Leaf sections Light regulation Maize Phosphoenolpyruvate carboxykinase Phosphorylation sites |
| ISSN号 | 0167-4412 |
| DOI | 10.1007/s11103-014-0171-3 |
| 文献子类 | Article |
| 英文摘要 | 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. |
| 学科主题 | Biochemistry & Molecular Biology ; Plant Sciences |
| 出版地 | DORDRECHT |
| 电子版国际标准刊号 | 1573-5028 |
| WOS关键词 | BUNDLE SHEATH-CELLS ; CRASSULACEAN ACID METABOLISM ; C-4 PHOTOSYNTHESIS ; PANICUM-MAXIMUM ; PLANT-TISSUES ; ZEA-MAYS ; DECARBOXYLATION ; MESOPHYLL ; ASPARTATE ; PROTEINS |
| WOS研究方向 | Biochemistry & Molecular Biology ; Plant Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000335756900007 |
| 出版者 | SPRINGER |
| 资助机构 | National Natural Science Fund of China [31030017] ; National Basic Research Program of China [2009CB118601] ; National Key Technology Support Program of China [2011BAD16B14] ; Shanghai Science and Technology Committee [12DZ2272100] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/27303]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.[Chao, Qing 2.Mei, Ying-Chang 3.Gao, Zhi-Fang 4.Chen, Yi-Bo 5.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing 100093, Peoples R China 6.Northeast Forestry Univ, State Key Lab Forest Genet & Tree Breeding, Harbin 150040, Peoples R China 7.[Qian, Chun-Rong 8.Heilongjiang Acad Agr Sci, Inst Crop Cultivat & Farming, Harbin 150086, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chao, Qing,Liu, Xiao-Yu,Mei, Ying-Chang,et al. Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity[J]. PLANT MOLECULAR BIOLOGY,2014,85(1-2):95-105. |
| APA | Chao, Qing.,Liu, Xiao-Yu.,Mei, Ying-Chang.,Gao, Zhi-Fang.,Chen, Yi-Bo.,...&Wang, Bai-Chen.(2014).Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity.PLANT MOLECULAR BIOLOGY,85(1-2),95-105. |
| MLA | Chao, Qing,et al."Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity".PLANT MOLECULAR BIOLOGY 85.1-2(2014):95-105. |
入库方式： OAI收割
来源：植物研究所
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