蛋白质组范围内赖氨酸 2-羟基异丁酰化的鉴定揭示了Physcomitrella patens 中保守和新的组蛋白修饰。
Proteome-wide identification of lysine 2-hydroxyisobutyrylation reveals conserved and novel histone modifications in Physcomitrella patens.
机构信息
College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 310018, China.
Department of Molecular Cellular and Developmental Biology, College of Letters & Science, University of California, Santa Barbara, CA, 93116, USA.
出版信息
Sci Rep. 2017 Nov 14;7(1):15553. doi: 10.1038/s41598-017-15854-z.
Protein lysine 2-hydroxyisobutyrylation (K) is a newly identified post-translational modification found in animal and yeast cells. Previous research suggested that histone K is involved in male cell differentiation and plays a critical role in the regulation of chromatin functions in animals. However, information regarding protein K in plants is still limited. In this study, using a specific antibody and LC-MS/MS methods, we identified 11,976 K sites in 3,001 proteins in Physcomitrella patens. The bioinformatics analysis indicated that these K-modified proteins were involved in a wide range of molecular functions and cellular processes, and showed diverse subcellular localizations. Furthermore, an comparism of K sites in histone proteins among human, mouse and P. patens found conserved sites in the H3 and H4 histone proteins and novel sites in H1, H2A and H2B histone proteins in P. patens. This is the first report on K post-translational modifications in plants, and the study provides a comprehensive profile of K sites in histone and non-histone proteins in Physcomitrella patens.
蛋白质赖氨酸 2-羟异丁酰化（K）是一种新发现的在动物和酵母细胞中存在的翻译后修饰。先前的研究表明，组蛋白 K 参与雄性细胞分化，并在动物染色质功能的调控中发挥关键作用。然而，关于植物中蛋白质 K 的信息仍然有限。在这项研究中，我们使用特定的抗体和 LC-MS/MS 方法，在Physcomitrella patens 中鉴定了 3001 种蛋白质中的 11976 个 K 位点。生物信息学分析表明，这些 K 修饰的蛋白质参与了广泛的分子功能和细胞过程，并显示出多样化的亚细胞定位。此外，对人类、小鼠和 P. patens 中组蛋白蛋白中的 K 位点进行比较，发现 P. patens 中的 H3 和 H4 组蛋白蛋白中有保守的位点，而 H1、H2A 和 H2B 组蛋白蛋白中有新的位点。这是首次在植物中报道 K 翻译后修饰，该研究提供了 Physcomitrella patens 中组蛋白和非组蛋白蛋白中 K 位点的全面概况。
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