Quantitative Proteomic Approaches to Studying Histone Modifications
Barry M Zee, Nicolas L Young, Benjamin A Garcia*
Identifiers and Pagination:Year: 2011
Issue: Suppl 1
First Page: 106
Last Page: 114
Publisher Id: CCGTM-5-106
Article History:Received Date: 4/12/2010
Revision Received Date: 26/3/2011
Acceptance Date: 25/4/2011
Electronic publication date: 22/8/2011
Collection year: 2011
open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
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.