Probing the acetylation code of histone H4

Diana Lang, Michael Schümann, Kathy Gelato, Wolfgang Fischle, Dirk Schwarzer*, Eberhard Krause

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2989-2997
Number of pages9
JournalProteomics
Volume13
Issue number20
DOIs
StatePublished - Oct 1 2013

Keywords

  • Cell biology
  • Chromatin
  • Histone acetylation
  • Interactome analysis
  • Quantitative mass spectrometry
  • SILAC

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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