Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation
- Author:
Gao ZHI-FANG
1
,
2
;
Shen ZHUO
;
Chao QING
;
Yan ZHEN
;
Ge XUAN-LIANG
;
Lu TIANCONG
;
Zheng HAIYAN
;
Qian CHUN-RONG
;
Wang BAI-CHEN
Author Information
1. Key Laboratory of Photobiology,CAS,Institute of Botany,Chinese Academy of Sciences,Beijing 100093,China
2. University of Chinese Academy of Sciences,Beijing 100049,China
- Keywords:
Maize seedling leaves;
De-etiolation;
Quantitative analysis;
Proteome;
Phosphoproteome
- From:
Genomics, Proteomics & Bioinformatics
2020;18(4):397-414
- CountryChina
- Language:Chinese
-
Abstract:
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, trig-gers the inhibition of mesocotyl elongation and the production of photosynthetically active chloro-plasts, 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 pro-teins 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 con-trast, 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 anal-ysis, 34.0％(1057/3110) of phosphorylated proteins identified in this study contained more than 2phosphorylation 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.
