Combined Metabolic and Chemical (CoMetChem) labeling using stable isotopes

Histone acetylation is an important, reversible posttranslational protein modification and hallmark of epigenetic regulation. However, little is known about the dynamics of reversible hisotne acetylation, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride, which allows to quantify site-specific lysine acetylation dynamics in tryptic peptides using high-resolution mass spectrometry.