ChIP-seq of MYST acetyltransferases
Histone acetyltransferases (HAT) assemble into multisubunit complexes in order to target distinct lysine residues on nucleosomal histones.  Here, we characterize native HAT complexes assembled by the BRPF-family of scaffold proteins.  Their PHD-ZnKnuckle-PHD domain is essential for binding chromatin and restricted to unmethylated H3K4, a specificity that is reversed by the associated ING subunit.  Native BRPF1 complexes can contain either MOZ/MORF or HBO1 as catalytic acetyltransferase subunit.  Interestingly, while the previously reported HBO1 complexes containing JADE scaffold proteins target histone H4, the HBO1-BRPF1 complex acetylates only H3 in chromatin.  We mapped a small region at the N-terminus of scaffold proteins responsible for histone tail selection on chromatin.  Thus, alternate choice of subunits associated with HBO1 can switch its specificity from H4 to H3 tails, highlighting a crucial new role of associated subunits within HAT complexes, previously thought to be intrinsic to the catalytic subunit. Overall design: Genome-wide mapping of MYST acetyltransferases subunits and H3K4me3 histone mark in RKO cells.