3Q35

Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

3Q35 の概要

• エントリーDOI: 10.2210/pdb3q35/pdb
• 関連するPDBエントリー: 3D35 3DM7 3Q33
• 分子名称: Histone acetyltransferase, Vacuolar protein sorting-associated protein 75, ACETYL COENZYME *A, ... (5 entities in total)
• 機能のキーワード: rtt109:vps75=2:2 stoichiometry complex, acetyl coenzyme a (acoa) bound, autoacetylation at rtt109 lys290, nuclear, transferase-chaperone complex, transferase/chaperone
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78513.22

構造登録者

Tang, Y.,Yuan, H.,Meeth, K.,Marmorstein, R. (登録日: 2010-12-21, 公開日: 2011-02-02, 最終更新日: 2024-11-06)

主引用文献

Tang, Y.,Holbert, M.A.,Delgoshaie, N.,Wurtele, H.,Guillemette, B.,Meeth, K.,Yuan, H.,Drogaris, P.,Lee, E.H.,Durette, C.,Thibault, P.,Verreault, A.,Cole, P.A.,Marmorstein, R.
Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation.
Structure, 19:221-231, 2011

PubMed Abstract: Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules to form a symmetrical holoenzyme with a ∼12 Å diameter central hole. Vps75 and Rtt109 residues that mediate complex formation in the crystals are also important for Rtt109-Vps75 interaction and H3K9/K27 acetylation both in vitro and in yeast cells. The same Rtt109 residues do not participate in Asf1-mediated Rtt109 acetylation in vitro or H3K56 acetylation in yeast cells, demonstrating that Asf1 and Vps75 dictate Rtt109 substrate specificity through distinct mechanisms. These studies also suggest that Vps75 binding stimulates Rtt109 catalytic activity by appropriately presenting the H3-H4 substrate within the central cavity of the holoenzyme to promote H3K9/K27 acetylation of new histones before deposition.

PubMed: 21256037
DOI: 10.1016/j.str.2010.12.012

実験手法

X-RAY DIFFRACTION (3.3 Å)