乙酰化生物学研究进展

发布时间：2018-11-13 16:58

【摘要】：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。
[Abstract]:Since the discovery of reversible protein acetylation modification, the previous 30 years have been limited to exploring histone acetylation modification involved in the regulation of chromatin remodeling and gene transcription, and the discovery of acetyltransferase (histone acetyltransferase,HAT) acting on histone. Deacetylase (histone deacetylase,HDAC) and deacetylase inhibitor (histone deacetylase inhibitors,HDACI). In recent ten years, with the discovery of acetylated non-histone and its related modifying enzymes in extracellular components, reversible acetylation modification has been gradually recognized in many cell life processes. However, the acetylation modification spectrum of proteins involved in complex biological processes is unclear. With the development of technology, acetylation modification can be identified and quantitatively analyzed at the whole proteomics level. These results reveal the complexity of acetylation and suggest that acetylation may be as common as phosphorylation and play an important role in the regulation of biological processes. Comprehensive protein acetylation identification is an area to be further explored, which will provide more comprehensive and valuable information on protein acetylation modification spectrum.
【作者单位】：重庆医科大学附属第一医院神经内科;重庆医科大学基础医学院神经科学研究中心;重庆医科大学药学院药理学实验室;
【基金】：国家“973”资助项目(编号:2009CB918300)
【分类号】：R341

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