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Probing the acetylation code of histone H 4
Author(s) -
Lang Diana,
Schümann Michael,
Gelato Kathy,
Fischle Wolfgang,
Schwarzer Dirk,
Krause Eberhard
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200568
Subject(s) - acetylation , histone h4 , histone , code (set theory) , computational biology , histone code , biology , genetics , computer science , programming language , dna , nucleosome , gene , set (abstract data type)
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 H 4. Quantitative peptide‐based affinity MS experiments using the SILAC approach determined the interactomes of H 4 tails monoacetylated at the four known acetylation sites K 5, K 8, K 12, and K 16, bis‐acetylated at K 5/ K 12, triple‐acetylated at K 8/12/16 and fully tetra‐acetylated. A set of 29 proteins was found enriched on the fully acetylated H 4 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 H 4 acetylation state establishes its regulatory effects in a cumulative manner rather than via site‐specific recruitment of regulatory proteins.