Yuan Zuo-Fei, Arnaudo Anna M, Garcia Benjamin A
Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104; email:
Annu Rev Anal Chem (Palo Alto Calif). 2014;7(1):113-28. doi: 10.1146/annurev-anchem-071213-015959. Epub 2014 Jun 2.
Histones play important roles in chromatin, in the forms of various posttranslational modifications (PTMs) and sequence variants, which are called histone proteoforms. Investigating modifications and variants is an ongoing challenge. Previous methods are based on antibodies, and because they usually detect only one modification at a time, they are not suitable for studying the various combinations of modifications on histones. Fortunately, mass spectrometry (MS) has emerged as a high-throughput technology for histone analysis and does not require prior knowledge about any modifications. From the data generated by mass spectrometers, both identification and quantification of modifications, as well as variants, can be obtained easily. On the basis of this information, the functions of histones in various cellular contexts can be revealed. Therefore, MS continues to play an important role in the study of histone proteoforms. In this review, we discuss the analysis strategies of MS, their applications on histones, and some key remaining challenges.
组蛋白以各种翻译后修饰（PTM）和序列变体的形式在染色质中发挥重要作用，这些被称为组蛋白蛋白质变体。研究修饰和变体是一项持续存在的挑战。以前的方法基于抗体，由于它们通常一次只能检测一种修饰，因此不适用于研究组蛋白上修饰的各种组合。幸运的是，质谱（MS）已成为一种用于组蛋白分析的高通量技术，并且不需要关于任何修饰的先验知识。从质谱仪产生的数据中，可以轻松获得修饰以及变体的鉴定和定量。基于这些信息，可以揭示组蛋白在各种细胞环境中的功能。因此，质谱在组蛋白蛋白质变体的研究中继续发挥重要作用。在这篇综述中，我们讨论了质谱的分析策略、它们在组蛋白上的应用以及一些仍然存在的关键挑战。
