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Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation
Genomics, Proteomics & Bioinformatics ( IF 9.5 ) Pub Date : 2020-12-30 , DOI: 10.1016/j.gpb.2020.12.004
Zhi-Fang Gao 1 , Zhuo Shen 2 , Qing Chao 3 , Zhen Yan 1 , Xuan-Liang Ge 4 , Tiancong Lu 5 , Haiyan Zheng 6 , Chun-Rong Qian 4 , Bai-Chen Wang 1
Affiliation  

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.



中文翻译:

去黄化过程中玉米幼苗叶片的大规模蛋白质组学和磷酸蛋白质组学分析

去黄化包括植物响应光而经历的一系列发育和生理变化。在这个过程中,光这一重要的环境信号触发了中胚轴伸长的抑制和光合活性叶绿体的产生,并使黄化的叶片从“汇”阶段过渡到“源”阶段。已在玉米中广泛研究了去黄化(Zea maysL.)。然而,人们对如何调节这种转变知之甚少。在这项研究中,我们描述了玉米去黄化过程的定量蛋白质组学和磷酸蛋白质组学图谱。我们在蛋白质组中鉴定了 16,420 种蛋白质,其中 14,168 种蛋白质被量化。此外,还鉴定了 3110 种蛋白质中的 8746 个磷酸化位点。从组合的蛋白质组学和磷酸蛋白质组学数据中,我们共鉴定了 17,436 种蛋白质。在去黄化过程中,只有 7.0% (998/14,168) 的蛋白质丰度发生了显着变化。相比之下,26.6% 的磷酸化蛋白表现出磷酸化水平的显着变化;这些包括参与基因表达和稳态途径的蛋白质以及参与光合光和碳反应的限速酶。基于磷酸蛋白质组学分析,34。本研究中鉴定的磷酸化蛋白中有 0% (1057/3110) 含有超过 2 个磷酸化位点,37 种蛋白质含有超过 16 个磷酸化位点,表明多磷酸化在去黄化过程中无处不在。我们的研究结果表明,植物可能会优先调节翻译后修饰 (PTM) 的水平,而不是蛋白质丰度,以适应不断变化的环境。因此,对 PTM 的研究可以更好地揭示去黄化的调节。我们的研究结果表明,植物可能会优先调节翻译后修饰 (PTM) 的水平,而不是蛋白质丰度,以适应不断变化的环境。因此,对 PTM 的研究可以更好地揭示去黄化的调节。我们的研究结果表明,植物可能会优先调节翻译后修饰 (PTM) 的水平,而不是蛋白质丰度,以适应不断变化的环境。因此,对 PTM 的研究可以更好地揭示去黄化的调节。

更新日期:2020-12-30
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