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  Probing the acetylation code of histone H4.

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.

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 Creators:
Lang, D., Author
Schümann, M., Author
Gelato, K.1, Author           
Fischle, W.1, Author           
Schwarzer, D., Author
Krause, E., Author
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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Free keywords: Cell biology / Chromatin / Histone acetylation / Interactome analysis / Quantitative mass spectrometry / SILAC
 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.

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Language(s): eng - English
 Dates: 2013-10-082013-10
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/pmic.201200568
 Degree: -

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Title: Proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 13 (20) Sequence Number: - Start / End Page: 2989 - 2997 Identifier: -