Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation

doi:10.1016/j.gpb.2020.12.004

CORC > 植物研究所 > 中国科学院植物研究所 > 中科院光生物学重点实验室

	Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation
	Gao, Zhi-Fang ; Shen, Zhuo 2; Chao, Qing ; Yan, Zhen ; Ge, Xuan-Liang ; Lu, Tiancong 4; Zheng, Haiyan 5; Qian, Chun-Rong ; Wang, Bai-Chen
刊名	GENOMICS PROTEOMICS & BIOINFORMATICS
	2020
卷号	18 期号:4 页码:397-414
关键词	Maize seedling leaves De-etiolation Quantitative analysis Proteome Phosphoproteome
ISSN号	1672-0229
DOI	10.1016/j.gpb.2020.12.004
文献子类	Article
英文摘要	De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light. During this process light, an important environmental signal, triggers the inhibition of mesocotyl elongation and the production of photosynthetically active chloroplasts, and etiolated leaves transition from the sink stage to the source stage. De-etiolation has been extensively studied in maize (Zea mays L.). However, little is known about how this transition is regulated. In this study, we described a quantitative proteomic and phosphoproteomic atlas of the de-etiolation process in maize. We identified 16,420 proteins in proteome, among which 14,168 proteins were quantified. In addition, 8746 phosphorylation sites within 3110 proteins were identified. From the combined proteomic and phosphoproteomic data, we identified a total of 17,436 proteins. Only 7.0% (998/14,168) of proteins significantly changed in abundance during de-etiolation. In contrast, 26.6% of phosphorylated proteins exhibited significant changes in phosphorylation level; these included proteins involved in gene expression and homeostatic pathways and rate-limiting enzymes involved in photosynthetic light and carbon reactions. Based on phosphoproteomic analysis, 34.0% (1057/3110) of phosphorylated proteins identified in this study contained more than 2 phosphorylation sites, and 37 proteins contained more than 16 phosphorylation sites, indicating that multi-phosphorylation is ubiquitous during the de-etiolation process. Our results suggest that plants might preferentially regulate the level of posttranslational modifications (PTMs) rather than protein abundance for adapting to changing environments. The study of PTMs could thus better reveal the regulation of de-etiolation.
学科主题	Genetics & Heredity
电子版国际标准刊号	2210-3244
出版地	AMSTERDAM
WOS关键词	POSTTRANSLATIONAL MODIFICATIONS ; PROTEIN-PHOSPHORYLATION ; BLUE-LIGHT ; PLANT PHOSPHOPROTEOMICS ; SIGNAL TRANSDUCER ; ARABIDOPSIS CRY2 ; RICE SEEDLINGS ; BUNDLE-SHEATH ; PHYTOCHROME-A ; ACCLIMATION
WOS研究方向	Genetics & Heredity
语种	英语
出版者	ELSEVIER
WOS记录号	WOS:000667272600004
资助机构	National Key R AMP ; D Program of China [2016YFD0101003] ; Heilongjiang Provincial Outstanding Youth Science Foundation, China [JC2017008]
内容类型	期刊论文
源URL	[http://ir.ibcas.ac.cn/handle/2S10CLM1/21461]
专题	中科院光生物学重点实验室
作者单位	1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, CAS, Beijing 100093, Peoples R China 3.Guangdong Acad Agr Sci, Vegetable Res Inst, Guangdong Key Lab New Technol Res Vegetables, Guangzhou 510640, Peoples R China 4.Heilongjiang Acad Agr Sci, Inst Crop Cultivat & Farming, Harbin 150086, Peoples R China 5.Beijing Prot World Biotech, Beijing 100012, Peoples R China 6.Rutgers State Univ, Ctr Adv Biotechnol & Med, Biol Mass Spectrometry Facil, Piscataway, NJ 08855 USA
推荐引用方式 GB/T 7714	Gao, Zhi-Fang,Shen, Zhuo,Chao, Qing,et al. Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation[J]. GENOMICS PROTEOMICS & BIOINFORMATICS,2020,18(4):397-414.
APA	Gao, Zhi-Fang.,Shen, Zhuo.,Chao, Qing.,Yan, Zhen.,Ge, Xuan-Liang.,...&Wang, Bai-Chen.(2020).Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation.GENOMICS PROTEOMICS & BIOINFORMATICS,18(4),397-414.
MLA	Gao, Zhi-Fang,et al."Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation".GENOMICS PROTEOMICS & BIOINFORMATICS 18.4(2020):397-414.