8OOT

CryoEM Structure INO80core Hexasome complex Arp5 Ies6 refinement state2

8OOT の概要

• エントリーDOI: 10.2210/pdb8oot/pdb
• EMDBエントリー: 17025 17026 17028 17029
• 分子名称: Chromatin-remodeling complex subunit IES6, Actin-related protein 5, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: atp-dependent chromatin remodeler, dna binding protein
• 由来する生物種: Thermochaetoides thermophila; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111432.09

構造登録者

Zhang, M.,Jungblut, A.,Hoffmann, T.,Eustermann, S. (登録日: 2023-04-05, 公開日: 2023-07-26, 最終更新日: 2024-07-24)

主引用文献

Zhang, M.,Jungblut, A.,Kunert, F.,Hauptmann, L.,Hoffmann, T.,Kolesnikova, O.,Metzner, F.,Moldt, M.,Weis, F.,DiMaio, F.,Hopfner, K.P.,Eustermann, S.
Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.
Science, 381:313-319, 2023

PubMed Abstract: Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of noncanonical nucleosomal particles remains largely elusive. In this work, we report the structural mechanism for adenosine 5'-triphosphate-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes noncanonical DNA and histone features of hexasomes that emerge from the loss of H2A-H2B. A large structural rearrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. Our findings reveal how the loss of H2A-H2B grants remodelers access to a different, yet unexplored layer of energy-driven chromatin regulation.

PubMed: 37384673
DOI: 10.1126/science.adf6287

実験手法

ELECTRON MICROSCOPY (2.85 Å)