Proteome-wide lysine acetylation identification in developing rice (Oryza sativa) seeds and protein co-modification by acetylation, succinylation, ubiquitination, and phosphorylation

文献类型： 外文期刊

第一作者： Meng, Xiaoxi

作者： Meng, Xiaoxi;Lv, Yuanda;Mujahid, Hana;Peng, Zhaohua;Lv, Yuanda;Zhao, Han;Edelmann, Mariola J.;Peng, Xiaojun

作者机构：

关键词： Acetylome;Rice;Seeds;Lysine acetylation;Post-translational modification

期刊名称：BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS （ 影响因子：3.036； 五年影响因子：2.969 ）

ISSN： 1570-9639

年卷期： 2018 年 1866 卷 3 期

页码：

收录情况： SCI

摘要： Protein lysine acetylation is a highly conserved post-translational modification with various biological functions. However, only a limited number of acetylation sites have been reported in plants, especially in cereals, and the function of non-histone protein acetylation is still largely unknown. In this report, we identified 1003 lysine acetylation sites in 692 proteins of developing rice seeds, which greatly extended the number of known acetylated sites in plants. Seven distinguished motifs were detected flanking acetylated lysines. Functional annotation analyses indicated diverse biological processes and pathways engaged in lysine acetylation. Remarkably, we found that several key enzymes in storage starch synthesis pathway and the main storage proteins were heavily acetylated. A comprehensive comparison of the rice acetylome, succinylome, ubiquitome and phosphorylome with available published data was conducted. A large number of proteins carrying multiple kinds of modifications were identified and many of these proteins are known to be key enzymes of vital metabolic pathways. Our study provides extending knowledge of protein acetylation. It will have critical reference value for understanding the mechanisms underlying PTM mediated multiple signal integration in the regulation of metabolism and development in plants.

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