原创力文档a combination of h2a.z and h4 acetylation recruits brd2 to chromatin during transcriptional activationh2a的组合。.pdfVIP
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a combination of h2a.z and h4 acetylation recruits brd2 to chromatin during transcriptional activationh2a的组合。
A Combination of H2A.Z and H4 Acetylation Recruits
Brd2 to Chromatin during Transcriptional Activation
1,2 3 1 1 1,2
Ryan Draker , Marlee K. Ng , Elizabeth Sarcinella , Vladimir Ignatchenko , Thomas Kislinger ,
Peter Cheung1,2,3¤*
1 Ontario Cancer Institute, Toronto, Canada, 2 Department of Medical Biophysics, University of Toronto, Toronto, Canada, 3 Department of Biology, York University,
Toronto, Canada
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 found that Brd2’s preference for
H2A.Z nucleosomes is mediated through a combination of hyperacetylated H4 on these nucleosomes, as well as additional
features on H2A.Z itself. In addition, comparison of nucleosomes containing either H2A.Z-1 or H2A.Z-2 isoforms showed that
significantly more Brd2 co-purifies with the former, suggesting these two isoforms engage different downstream effector
proteins. Cons
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