title: Probing the acetylation code of histone H4.
abstract: 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.
authors: Laboratory of Mass Spectrometry, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
authors: Diana
authors: D
authors: Lang
authors: Michael
authors: M
authors: Schümann
authors: Kathy
authors: K
authors: Gelato
authors: Wolfgang
authors: W
authors: Fischle
authors: Dirk
authors: D
authors: Schwarzer
authors: Eberhard
authors: E
authors: Krause
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D015153:Blotting, Western; D006367:HeLa Cells; D042421:Histone Code; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007553:Isotope Labeling; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D015203:Reproducibility of Results
chemical_list: D006657:Histones; D010455:Peptides
keywords: Cell biology; Chromatin; Histone acetylation; Interactome analysis; Quantitative mass spectrometry; SILAC