byLang D., Schümann M., Gelato K., Fischle W., Schwarzer D., Krause E.
Lang D., Schümann M., Gelato K., Fischle W., Schwarzer D. and Krause E. (2013) Probing the acetylation code of histone H4. Proteomics 13:2989-2997
Histone modifications play crucial roles in genome regulation with lysine acetylation being implicated in transcriptional control. Here we report a proteome-wide investigation of the acetylation-dependent protein-protein interactions of the N-terminal tail of histone H4. Quantitative peptide-based affinity MS experiments using the SILAC approach determined the interactomes of H4 tails monoacetylated at the four known acetylation sites K5, K8, K12, and K16, bis-acetylated at K5/K12, triple-acetylated at K8/12/16 and fully tetra-acetylated. A set of 29 proteins was found enriched on the fully acetylated H4 tail while specific binders of the mono and bis-acetylated tails were barely detectable. These observations are in good agreement with earlier reports indicating that the H4 acetylation state establishes its regulatory effects in a cumulative manner rather than via site-specific recruitment of regulatory proteins.
Cell biologyChromatinHistone acetylationInteractome analysisQuantitative mass spectrometrySILAC