修饰特异性蛋白质组学：利用富集技术对翻译后修饰进行特征描述的策略。
Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques.
机构信息
The Ben May Department for Cancer Research, The University of Chicago, Chicago, IL, USA.
出版信息
Proteomics. 2009 Oct;9(20):4632-41. doi: 10.1002/pmic.200900398.
Abstract
More than 300 different types of protein post-translational modifications (PTMs) have been described, many of which are known to have pivotal roles in cellular physiology and disease. Nevertheless, only a handful of PTMs have been extensively investigated at the proteome level. Knowledge of protein substrates and their PTM sites is key to dissection of PTM-mediated cellular processes. The past several years have seen a tremendous progress in developing MS-based proteomics technologies for global PTM analysis, including numerous studies of yeast and other microbes. Modification-specific enrichment techniques combined with advanced MS/MS methods and computational data analysis have revealed a surprisingly large extent of PTMs in proteins, including multi-site, cooperative modifications in individual proteins. We review some of the current strategies employed for enrichment and detection of PTMs in modification-specific proteomics.
摘要
已经描述了 300 多种不同类型的蛋白质翻译后修饰（PTM），其中许多已知在细胞生理学和疾病中起着关键作用。然而，只有少数 PTM 在蛋白质组水平上得到了广泛研究。了解蛋白质底物及其 PTM 位点是解析 PTM 介导的细胞过程的关键。在过去的几年中，基于 MS 的蛋白质组学技术在全球 PTM 分析方面取得了巨大进展，包括对酵母和其他微生物的多项研究。修饰特异性富集技术与先进的 MS/MS 方法和计算数据分析相结合，揭示了蛋白质中 PTM 的惊人程度，包括单个蛋白质中的多部位、协同修饰。我们回顾了一些当前用于修饰特异性蛋白质组学中 PTM 富集和检测的策略。
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