7YFP

The NuA4 histone acetyltransferase complex from S. cerevisiae

7YFP の概要

• エントリーDOI: 10.2210/pdb7yfp/pdb
• EMDBエントリー: 33796
• 分子名称: Actin, ARP4 isoform 1, Chromatin modification-related protein EAF1, ... (7 entities in total)
• 機能のキーワード: histone acetyltransferase, h4, acetylation, nua4, nucleosome, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 794462.88

構造登録者

Ji, L.T.,Zhao, L.X.,Xu, K.,Gao, H.H.,Zhou, Y.,Kornberg, R.D.,Zhang, H.Q. (登録日: 2022-07-08, 公開日: 2023-04-19)

主引用文献

Ji, L.,Zhao, L.,Xu, K.,Gao, H.,Zhou, Y.,Kornberg, R.D.,Zhang, H.
Structure of the NuA4 histone acetyltransferase complex.
Proc.Natl.Acad.Sci.USA, 119:e2214313119-e2214313119, 2022

PubMed Abstract: Nucleosome acetyltransferase of H4 (NuA4), one of two major histone acetyltransferase complexes in  specifically acetylates histone H2A and H4, resulting in increased transcriptional activity. Here we present a 3.8-4.0 Å resolution structure of the NuA4 complex from cryoelectron microscopy and associated biochemical studies. The determined structure comprises six subunits and appropriately 5,000 amino acids, with a backbone formed by subunits Eaf1 and Eaf2 spanning from an Actin-Arp4 module to a platform subunit Tra1. Seven subunits are missing from the cryo-EM map. The locations of missing components, Yaf9, and three subunits of the Piccolo module Esa1, Yng2, and Eaf6 were determined. Biochemical studies showed that the Piccolo module and the complete NuA4 exhibit comparable histone acetyltransferase activities, but the Piccolo module binds to nucleosomes, whereas the complete NuA4 does not. The interaction lifetime of NuA4 and nucleosome is evidently short, possibly because of subunits of the NuA4 complex that diminish the affinity of the Piccolo module for the nucleosome, enabling rapid movement from nucleosome to nucleosome.

PubMed: 36417436
DOI: 10.1073/pnas.2214313119

実験手法

ELECTRON MICROSCOPY (4 Å)