Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity
文献类型：期刊论文
| 作者 | 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 |
| 刊名 | PLANT PHYSIOLOGY
 |
| 出版日期 | 2014 |
| 卷号 | 165期号:2页码:534-549 |
| ISSN号 | 0032-0889 |
| DOI | 10.1104/pp.113.231993 |
| 文献子类 | Article |
| 英文摘要 | 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. |
| 学科主题 | Plant Sciences |
| 出版地 | ROCKVILLE |
| 电子版国际标准刊号 | 1532-2548 |
| 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 |
| 语种 | 英语 |
| WOS记录号 | WOS:000337242700006 |
| 出版者 | AMER SOC PLANT BIOLOGISTS |
| 资助机构 | State Key Program of National Natural Science of China [31030017] ; National Natural Science of China [31270347] |
| 源URL | [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 |
| 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. |
入库方式： OAI收割
来源：植物研究所
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