Application of mass spectrometry to the identification and quantification of histone post-translational modifications

被引:107
作者
Freitas, MA
Sklenar, AR
Parthun, MR [1 ]
机构
[1] Ohio State Univ, Dept Mol & Cellular Biochem, Columbus, OH 43210 USA
[2] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA
关键词
chromatin; mass spectrometry; histone; post-translational modification;
D O I
10.1002/jcb.20106
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The core histones are the primary p rote in component of chromatin, which is responsible forth e packaging of eukaryotic DNA. The NH2-terminal tail domains of the core histones are the sites of numerous post-translational modifications that have been shown to play an important role in the regulation of chromatin structure. In this study, we discuss the recent application of modern analytical techniques to the study of histone modifications. Through the use of mass spectrometry, a large number of new sites of histone modification have been identified, many of which reside outside of the NH2-terrninal tail domains. In addition, techniques have been developed that allow mass spectrometry to be effective for the quantitation of histone post-translational modifications. Hence, the use of mass spectrometry promises to dramatically alter our view of histone post-translational modifications. (C) 2004 Wiley-Liss, Inc.
引用
收藏
页码:691 / 700
页数:10
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