Protein lysine acetylation analysis: current MS-based proteomic technologies.
Protein lysine acetylation analysis: current MS-based proteomic technologies.
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DOI：
10.1039/c3an36837h
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发表时间：
2013-02
期刊：
影响因子：
--
通讯作者：
Kai Zhang;Shanshan Tian;Enguo Fan
中科院分区：
文献类型：
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作者：
Kai Zhang;Shanshan Tian;Enguo Fan
蛋白质赖氨酸乙酰化（Kac）包括组蛋白乙酰化和非核蛋白乙酰化，是一种动态的、可逆的翻译后修饰，具有细胞调控作用。修饰的蛋白质在调节染色质结构、转录活性和代谢途径中起关键作用，从而有助于多种细胞过程，如转录、细胞周期调节、凋亡和衰老。因此，靶向蛋白质乙酰化代表了用于某些疾病（例如癌症）的潜在有前途的策略。然而，由于蛋白质乙酰化的动态特性和相对低的丰度，其全局识别是一个主要的瓶颈。为了从不同的细胞来源开发基于质谱（MS）的蛋白质组学技术，已经做出了巨大的努力。本综述试图提供一个概述目前的策略用于Kac鉴定从组蛋白到全系统的Kac分析，包括富集技术，色谱分离策略，和质谱方法。
Protein lysine acetylation (Kac), including histone acetylation and non-nuclear protein acetylation, is a dynamic and reversible post-translational modification for cellular regulation. The modified proteins play a key role in regulating chromatin structure, transcriptional activity and metabolic pathways, thus contributing to diverse cellular processes like transcription, cell cycle regulation, apoptosis and senescence. Therefore, targeting protein acetylation represents a potentially promising strategy for certain diseases, such as cancer. However, global identification of protein acetylation is a major bottleneck due to its dynamic property and rather low abundance. Tremendous efforts have been made to develop mass spectrometry (MS)-based proteomic technologies for this purpose from diverse cellular sources. The present review has tried to provide an overview of current strategies employed for Kac identification from histone to system-wide Kac analysis, including enrichment techniques, chromatographic separation strategies, and mass spectrometry methods.