2r0s
Crystal Structure of the Rsc4 tandem bromodomain
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OverviewOverview
An important issue for chromatin remodeling complexes is how their, bromodomains recognize particular acetylated lysine residues in histones., The Rsc4 subunit of the yeast remodeler RSC contains an essential tandem, bromodomain (TBD) that binds acetylated K14 of histone H3 (H3K14ac). We, report a series of crystal structures that reveal a compact TBD that binds, H3K14ac in the second bromodomain and, remarkably, binds acetylated K25 of, Rsc4 itself in the first bromodomain. Endogenous Rsc4 is acetylated only, at K25, and Gcn5 is identified as necessary and sufficient for Rsc4 K25, acetylation in vivo and in vitro. Rsc4 K25 acetylation inhibits binding to, H3K14ac, and mutation of Rsc4 K25 results in altered growth rates. These, data suggest an autoregulatory mechanism in which Gcn5 performs both the, activating (H3K14ac) and inhibitory (Rsc4 K25ac) modifications, perhaps to, provide temporal regulation. Additional regulatory mechanisms are, indicated as H3S10 phosphorylation inhibits Rsc4 binding to H3K14ac, peptides.
About this StructureAbout this Structure
2R0S is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation., VanDemark AP, Kasten MM, Ferris E, Heroux A, Hill CP, Cairns BR, Mol Cell. 2007 Sep 7;27(5):817-28. PMID:17803945
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