Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli
Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli
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DOI：
10.1074/mcp.m800187-mcp200
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发表时间：
2009-02-01
影响因子：
7
通讯作者：
Zhao, Yingming
中科院分区：
文献类型：
--
作者：
Zhang, Junmei;Sprung, Robert;Zhao, Yingming
赖氨酸乙酰化及其调控酶在哺乳动物细胞生理学中具有重要作用。然而，这种修饰在原核细胞中的程度和功能仍然在很大程度上未被探索，从而提出了一个障碍，以进一步在原核系统中的功能研究这种修饰。在这里，我们报告的第一个全球筛选赖氨酸乙酰化，确定138个修饰位点的91个蛋白质从大肠杆菌。以前没有蛋白质与这种修饰相关。在鉴定的蛋白质中有转录调节因子，以及其他具有不同功能的蛋白质。有趣的是，超过70%的乙酰化蛋白质是代谢酶和翻译调节剂，这表明这种修饰与能量代谢密切相关。新的数据集表明赖氨酸乙酰化在原核细胞中可能是丰富的。此外，这些结果也意味着赖氨酸乙酰化的功能超出了基因表达的调控是进化保守的从细菌到哺乳动物。此外，我们表明，细菌赖氨酸乙酰化调节应激刺激。Molecular & Cellular Proteomics 8：215-225，2009.
Lysine acetylation and its regulatory enzymes are known to have pivotal roles in mammalian cellular physiology. However, the extent and function of this modification in prokaryotic cells remain largely unexplored, thereby presenting a hurdle to further functional study of this modification in prokaryotic systems. Here we report the first global screening of lysine acetylation, identifying 138 modification sites in 91 proteins from Escherichia coli. None of the proteins has been previously associated with this modification. Among the identified proteins are transcriptional regulators, as well as others with diverse functions. Interestingly, more than 70% of the acetylated proteins are metabolic enzymes and translation regulators, suggesting an intimate link of this modification to energy metabolism. The new dataset suggests that lysine acetylation could be abundant in prokaryotic cells. In addition, these results also imply that functions of lysine acetylation beyond regulation of gene expression are evolutionarily conserved from bacteria to mammals. Furthermore, we demonstrate that bacterial lysine acetylation is regulated in response to stress stimuli. Molecular & Cellular Proteomics 8: 215-225, 2009.