Current Chemical Genomics and Translational Medicine

2011, 5 : 106-114
Published online 2011 August 22. DOI: 10.2174/1875397301005010106
Publisher ID: CCGTM-5-106

RESEARCH ARTICLE
 Quantitative Proteomic Approaches to Studying Histone Modifications

Barry M Zee , Nicolas L Young and Benjamin A Garcia, *
415 Schultz Laboratory, Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA

* Address correspondence to this author at 415 Schultz Laboratory, Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA; Tel: 609-258-1035; Fax: 609-258-8854; E-mail: bagarcia@princeton.edu

ABSTRACT

Histone post-translational modifications (PTMs) positively and negatively regulate gene expression, and are consequently a vital influence on the genomic profile of all eukaryotic species. The study of histone PTMs using classical methods in molecular biology, such as immunofluorescence and Western blotting, is challenging given the technical issues of the approaches, and chemical diversity and combinatorial patterns of the modifications. In light of these many technical limitations, mass spectrometry (MS) is emerging as the most unbiased and rigorous experimental platform to identify and quantify histone PTMs in a high-throughput manner. This review covers the latest developments in mass spectrometry for the analysis of histone PTMs, with the hope of inspiring the continued integration of proteomic, genomic and epigenetic research.

Keywords:

Histone, mass spectrometry, proteomic, modification epigenetic..