Mass Spectrometric Quantification of Histone Post-translational Modifications by a Hybrid Chemical Labeling Method[S]

• Published in: Molecular & cellular proteomics Vol. 14; no. 4; pp. 1148 - 1158
• Main Authors: Maile, Tobias M., Izrael-Tomasevic, Anita, Cheung, Tommy, Guler, Gulfem D., Tindell, Charles, Masselot, Alexandre, Liang, Jun, Zhao, Feng, Trojer, Patrick, Classon, Marie, Arnott, David
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.04.2015; The American Society for Biochemistry and Molecular Biology
• Subjects: Chromatography, Liquid; Gene Knockdown Techniques; HEK293 Cells; HeLa Cells; Histone Demethylases - metabolism; Histones - metabolism; Humans; Lysine - metabolism; Mass Spectrometry - methods; Methylation; Peptides - metabolism; Propionates - metabolism; Protein Processing, Post-Translational; Reference Standards; RNA, Small Interfering - metabolism; Staining and Labeling - methods; Technological Innovation and Resources; Trypsin - metabolism

Mass spectrometry is a powerful alternative to antibody-based methods for the analysis of histone post-translational modifications (marks). A key development in this approach was the deliberate propionylation of histones to improve sequence coverage across the lysine-rich and hydrophilic tails that...