A combination of H2A.Z and H4 acetylation recruits Brd2 to chromatin during transcriptional activation.

ABSTRACT: H2A.Z is an essential histone variant that has been implicated to have multiple chromosomal functions. To understand how H2A.Z participates in such diverse activities, we sought to identify downstream effector proteins that are recruited to chromatin via H2A.Z. For this purpose, we developed a nucleosome purification method to isolate H2A.Z-containing nucleosomes from human cells and used mass spectrometry to identify the co-purified nuclear proteins. Through stringent filtering, we identified the top 21 candidates, many of which have conserved structural motifs that bind post-translationally modified histones. We further validated the biological significance of one such candidate, Brd2, which is a double-bromodomain-containing protein known to function in transcriptional activation. We fo

SUBMITTER: Draker R 

PROVIDER: S-EPMC3493454 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature