Horticulture College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Life Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Sci Rep. 2020 Feb 12;10(1):2447. doi: 10.1038/s41598-020-59342-3.
Ubiquitination is a critical post-translational modification machinery that governs a wide range of cellular functions by regulating protein homeostasis. Identification of ubiquitinated proteins and lysine residues can help researchers better understand the physiological roles of ubiquitin modification in different biological systems. In this study, we report the first comprehensive analysis of the peach ubiquitome by liquid chromatography-tandem mass spectrometry-based diglycine remnant affinity proteomics. Our systematic profiling revealed a total of 544 ubiquitination sites on a total of 352 protein substrates. Protein annotation and functional analysis suggested that ubiquitination is involved in modulating a variety of essential cellular and physiological processes in peach, including but not limited to carbon metabolism, histone assembly, translation and vesicular trafficking. Our results could facilitate future studies on how ubiquitination regulates the agricultural traits of different peach cultivars and other crop species.
泛素化是一种关键的翻译后修饰机制，通过调节蛋白质稳态来控制广泛的细胞功能。鉴定泛素化蛋白和赖氨酸残基可以帮助研究人员更好地理解泛素修饰在不同生物系统中的生理作用。在这项研究中，我们通过基于液相色谱-串联质谱的二肽残基亲和蛋白质组学报告了桃泛素组的首次全面分析。我们的系统分析共揭示了 352 种蛋白质底物上的 544 个泛素化位点。蛋白质注释和功能分析表明，泛素化参与调节桃中多种重要的细胞和生理过程，包括但不限于碳代谢、组蛋白组装、翻译和囊泡运输。我们的研究结果将有助于未来研究泛素化如何调节不同桃品种和其他作物物种的农业性状。
