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

doi:10.1007/s11103-014-0171-3

IB-CAS > 中科院光生物学重点实验室

	Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity
	Chao, Qing ; Liu, Xiao-Yu ; Mei, Ying-Chang ; Gao, Zhi-Fang ; Chen, Yi-Bo ; Qian, Chun-Rong ; Hao, Yu-Bo ; Wang, Bai-Chen
	2014
发表期刊	PLANT MOLECULAR BIOLOGY
ISSN	0167-4412
卷号	85 期号:1-2 页码:95-105
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.
关键词	Enzyme activity Leaf sections Light regulation Maize Phosphoenolpyruvate carboxykinase Phosphorylation sites
学科领域	Biochemistry & Molecular Biology ; Plant Sciences
DOI	10.1007/s11103-014-0171-3
收录类别	SCI
语种	英语
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
WOS记录号	WOS:000335756900007
出版者	SPRINGER
文献子类	Article
出版地	DORDRECHT
EISSN	1573-5028
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]
作者邮箱	wangbc@ibcas.ac.cn
引用统计	被引频次：20[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	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.

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