Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology-KRIBB, Daejeon, Korea.
Proteomics. 2013 Aug;13(15):2278-82. doi: 10.1002/pmic.201200072. Epub 2013 Jul 11.
Recent analysis of prokaryotic N(ε)-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the N(ε)-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.
最近对原核 N(ε)-赖氨酸乙酰化蛋白的分析强调了广泛的细胞蛋白的翻译后调控。然而，由于原核生物中乙酰化蛋白质组数据的缺乏，乙酰化的确切作用仍不清楚。在这里，我们展示了革兰氏阳性嗜热菌 Geobacillus kaustophilus 的 N(ε)-赖氨酸乙酰化蛋白质组。使用乙酰-赖氨酸特异性抗体进行亲和富集，然后进行 LC-MS/MS 分析，揭示了 253 个乙酰化肽，代表 114 种蛋白质。这些乙酰化蛋白不仅包括来自嗜温菌 Bacillus 的常见同源物，还包括独特的 G. kaustophilus 蛋白，表明赖氨酸乙酰化在嗜热菌中很明显。这些数据补充了当前对细菌乙酰化蛋白质组的认识，并为更好地理解乙酰化在细胞代谢中的功能提供了一个扩展的平台。
