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Large-scale Identification and Time -course Quantification of Ubiquitylation Events During Maize Seedling De -etiolation

文献类型： 外文期刊

作者： Wang, Yue-Feng 1 ; Chao, Qing 1 ; Li, Zhe 3 ; Lu, Tian-Cong 4 ; Zheng, Hai-Yan 5 ; Zhao, Cai-Feng 5 ; Shen, Zhuo 1 ; Li, 1 ;

作者机构： 1.Chinese Acad Sci, Photosynth Res Ctr, Inst Bot, CAS Key Lab Photobiol, Beijing 100093, Peoples R China

2.Jilin Acad Agr Sci, Crop Germplasm Resources Inst, Gongzhuling 136100, Peoples R China

3.Precis Sci Beijing Co, Beijing 100085, Peoples R China

4.Univ Sci & Technol Beijing, Adv Biotechnol & Applicat Res Ctr, Sch Chem & Biol Engn, Beijing 100083, Peoples R China

5.Rutgers State Univ, Ctr Adv Biotechnol & Med, Biol Mass Spectrometry Facil, Piscataway, NJ 08855 USA

6.Grad Univ Chinese Acad Sci, Coll Life Sci, Beijing 100049, Peoples R China

关键词： Maize seedling leaf; De-etiolation; Ubiquitylation; C4 photosynthetic enzymes; Ribosome

期刊名称：GENOMICS PROTEOMICS & BIOINFORMATICS （ 影响因子：7.691； 五年影响因子：11.12 ）

ISSN： 1672-0229

年卷期： 2019 年 17 卷 6 期

页码：

收录情况： SCI

摘要： The ubiquitin system is crucial for the development and fitness of higher plants. De-etiolation, during which green plants initiate photomorphogenesis and establish autotrophy, is a dramatic and complicated process that is tightly regulated by a massive number of ubiquitylation/de-ubiquitylation events. Here we present site-specific quantitative proteomic data for the ubiquitylomes of de-etiolating seedling leaves of Zea mays L. (exposed to light for 1, 6, or 12 h) achieved through immunoprecipitation-based high-resolution mass spectrometry (MS). Through the integrated analysis of multiple ubiquitylomes, we identified and quantified 1926 unique ubiquitylation sites corresponding to 1053 proteins. We analyzed these sites and found five potential ubiquitylation motifs, KA, AXK, KXG, AK, and TK. Time-course studies revealed that the ubiquitylation levels of 214 sites corresponding to 173 proteins were highly correlated across two replicate MS experiments, and significant alterations in the ubiquitylation levels of 78 sites (fold change >1.5) were detected after de-etiolation for 12 h. The majority of the ubiquitylated sites we identified corresponded to substrates involved in protein and DNA metabolism, such as ribosomes and histones. Meanwhile, multiple ubiquitylation sites were detected in proteins whose functions reflect the major physiological changes that occur during plant de-etiolation, such as hormone synthesis/signaling proteins, key C4 photosynthetic enzymes, and light signaling proteins. This study on the ubiquitylome of the maize seedling leaf is the first attempt ever to study the ubiquitylome of a C4 plant and provides the proteomic basis for elucidating the role of ubiquitylation during plant de-etiolation.

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