Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity

doi:10.1104/pp.113.231993

IB-CAS > 中科院光生物学重点实验室

	Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity
	Chen, Yi-Bo ; Lu, Tian-Cong ; Wang, Hong-Xia ; Shen, Jie ; Bu, Tian-Tian ; Chao, Qing ; Gao, Zhi-Fang ; Zhu, Xin-Guang ; Wang, Yue-Feng ; Wang, Bai-Chen
	2014
发表期刊	PLANT PHYSIOLOGY
ISSN	0032-0889
卷号	165 期号:2 页码:534-549
摘要	In C-4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site threonine (Thr) residue; this process is catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. Here, we show that light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr-527 (previously termed Thr-456) of PPDK in maize (Zea mays). The amount of PPDK (unphosphorylated) involved in C-4 photosynthesis is indeed strictly controlled by light intensity, despite the high levels of PPDK protein that accumulate in mesophyll chloroplasts. In addition, we identified a transit peptide cleavage site, uncovered partial amino-terminal acetylation, and detected phosphorylation at four serine (Ser)/Thr residues, two of which were previously unknown in maize. In vitro experiments indicated that Thr-527 and Ser-528, but not Thr-309 and Ser-506, are targets of PDRP. Modeling suggests that the two hydrogen bonds between the highly conserved residues Ser-528 and glycine-525 are required for PDRP-mediated phosphorylation of the active-site Thr-527 of PPDK. Taken together, our results suggest that the regulation of maize plastid PPDK isoform (C4PPDK) activity is much more complex than previously reported. These diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in lighting.
学科领域	Plant Sciences
DOI	10.1104/pp.113.231993
收录类别	SCI
语种	英语
WOS关键词	NADP-MALATE DEHYDROGENASE ; ORTHO-PHOSPHATE DIKINASE ; C-4 PHOTOSYNTHESIS ; PHOSPHOENOLPYRUVATE CARBOXYKINASE ; PYRUVATE,ORTHOPHOSPHATE DIKINASE ; PI DIKINASE ; ZEA-MAYS ; PROTEIN ; EXPRESSION ; PHOSPHORYLATION
WOS研究方向	Plant Sciences
WOS记录号	WOS:000337242700006
出版者	AMER SOC PLANT BIOLOGISTS
文献子类	Article
出版地	ROCKVILLE
EISSN	1532-2548
资助机构	State Key Program of National Natural Science of China [31030017] ; National Natural Science of China [31270347]
作者邮箱	wangbc@ibcas.ac.cn
作品OA属性	Bronze, Green Published
引用统计	被引频次：36[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/2S10CLM1/27241
专题	中科院光生物学重点实验室
作者单位	1.[Chen, Yi-Bo 2.Shen, Jie 3.Bu, Tian-Tian 4.Chao, Qing 5.Gao, Zhi-Fang 6.Wang, Yue-Feng 7.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China 8.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Genom, Beijing 100101, Peoples R China 9.Chinese Acad Sci, Inst Genet & Dev Biol, Natl Ctr Plant Gene Res, Beijing 100101, Peoples R China 10.Natl Ctr Biomed Anal, Inst Basic Med Sci, Beijing 100850, Peoples R China 11.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China
推荐引用方式 GB/T 7714	Chen, Yi-Bo,Lu, Tian-Cong,Wang, Hong-Xia,et al. Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity[J]. PLANT PHYSIOLOGY,2014,165(2):534-549.
APA	Chen, Yi-Bo.,Lu, Tian-Cong.,Wang, Hong-Xia.,Shen, Jie.,Bu, Tian-Tian.,...&Wang, Bai-Chen.(2014).Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity.PLANT PHYSIOLOGY,165(2),534-549.
MLA	Chen, Yi-Bo,et al."Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity".PLANT PHYSIOLOGY 165.2(2014):534-549.

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
Chen-2014-Posttransl（2458KB）	期刊论文	出版稿	开放获取	CC BY-NC-SA	浏览请求全文