Characterization of histones and their post-translational modifications by mass spectrometry

被引:107
作者
Garcia, Benjamin A.
Shabanowitz, Jeffrey
Hunt, Donald F. [1 ]
机构
[1] Univ Illinois, Inst Genom Biol, Urbana, IL 61801 USA
[2] Univ Virginia, Dept Chem, Charlottesville, VA 22904 USA
[3] Univ Virginia, Ctr Hlth Sci, Dept Pathol, Charlottesville, VA 22908 USA
关键词
D O I
10.1016/j.cbpa.2006.11.022
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
Histone proteins and their accompanying post-translational modifications have received much attention for their ability to affect chromatin structure and, hence, regulate gene expression. Recently, mass spectrometry has become an important complementary tool for the analysis of histone variants and modification sites, for determining the degree of occupancy of these modifications and for quantifying differential expression of these modifications from various samples. Additionally, as advancements in mass spectrometry technologies continue, the ability to read entire 'histone codes' across large regions of histone polypeptides or intact protein is possible. As chromatin biology demands, mass spectrometry has adapted and continues as a key technology for the analysis of gene regulation networks involving histone modifications.
引用
收藏
页码:66 / 73
页数:8
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