English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Probing the acetylation code of histone H4.

MPS-Authors
/persons/resource/persons71700

Gelato,  K.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15074

Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)

1850500-Suppl-1.xlsx
(Supplementary material), 434KB

1850500-Suppl-2.xlsx
(Supplementary material), 367KB

1850500-Suppl-3.xlsx
(Supplementary material), 431KB

1850500-Suppl-4.xlsx
(Supplementary material), 406KB

1850500-Suppl-5.xlsx
(Supplementary material), 459KB

1850500-Suppl-6.xlsx
(Supplementary material), 526KB

1850500-Suppl-7.xlsx
(Supplementary material), 232KB

1850500-Suppl-8.xlsx
(Supplementary material), 277KB

Citation

Lang, D., Schümann, M., Gelato, K., Fischle, W., Schwarzer, D., & Krause, E. (2013). Probing the acetylation code of histone H4. Proteomics, 13(20), 2989-2997. doi:10.1002/pmic.201200568.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-7AA1-C
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.