乙酰化生物学研究进展

Protein acetylome:the emergencing acetylation biology

自从可逆性蛋白质乙酰化修饰发现以来,前30年的研究多局限于探索组蛋白乙酰化修饰参与染色质重塑和基因转录的调控,并发现了作用于组蛋白的乙酰转移酶(histone acetyltransferase,HAT)、去乙酰化酶(histone deacetylase,HDAC)及去乙酰化酶抑制剂(histone deacetylase inhibitors,HDACI)。近十年来,随着在细胞核外的细胞成分中发现乙酰化的非组蛋白及其相关的修饰酶,可逆性的乙酰化修饰在多种细胞生命过程中存在调控潜能逐渐得到认识。然而,复杂的生物学过程涉及到的蛋白质乙酰化修饰谱还不明确。由于技术的发展,目前已经可以在全蛋白质组学水平对乙酰化修饰进行鉴定和定量分析。这些研究结果揭示了乙酰化组学的复杂性,提出乙酰化修饰可能与磷酸化修饰一样普遍存在,并在生物学过程的调控中发挥着重要作用。全面的蛋白质乙酰化鉴定是一个有待继续探索的领域,将会提供更全面更有价值的蛋白质乙酰化修饰谱信息。

For the first 30 years since its discovery, reversible protein acetylation has been studied and understood almost exclusively in the context of chromatin remodeling and gene transcription accompanying the research of histone acetyltransferase （HAT）,histone deacetylase（HDAC） and HDAC inhibitors（HDACI）. With the discovery of non-histone acetylated proteins and acetylation-modifying enzymes in cellular compartments outside the nucleus, the regulatory potential in diverse cell progressing of reversible acetylation has slowly been recognized in the last decade. However,the scope of protein acetylation involvement in complex biological processes remains uncertain. The recent development of new technology has enabled, for the first time, the identification and quantification of the acetylome, acetylation events at the whole-proteome level. These efforts have uncovered a stunning complexity of the acetylome that potentially rivals that of the phosphoproteome. The remarkably ubiquitous and conserved nature of protein acetylation revealed by these new studies suggests the regulatory power of this dynamic modification. The establishment of comprehensive acetylomes will change the landscape of protein acetylation, where an exciting research frontier awaits.