2R0V

Structure of the Rsc4 tandem bromodomain acetylated at K25

2R0V の概要

• エントリーDOI: 10.2210/pdb2r0v/pdb
• 関連するPDBエントリー: 2R0S 2R0Y 2R10
• 分子名称: Chromatin structure-remodeling complex protein RSC4, SULFATE ION (3 entities in total)
• 機能のキーワード: bromodomain, chromatin, remodeler, rsc, histone, acetylation, transcription, chromatin regulator, nucleus, phosphorylation, transcription regulation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus : Q02206
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 120824.50

構造登録者

VanDemark, A.P.,Kasten, M.M.,Ferris, E.,Heroux, A.,Hill, C.P.,Cairns, B.R. (登録日: 2007-08-21, 公開日: 2007-10-30, 最終更新日: 2024-10-30)

主引用文献

VanDemark, A.P.,Kasten, M.M.,Ferris, E.,Heroux, A.,Hill, C.P.,Cairns, B.R.
Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation.
Mol.Cell, 27:817-828, 2007

PubMed Abstract: 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.

PubMed: 17803945
DOI: 10.1016/j.molcel.2007.08.018

実験手法

X-RAY DIFFRACTION (2.35 Å)