6R0C

Human-D02 Nucleosome Core Particle with biotin-streptavidin label

6R0C の概要

• エントリーDOI: 10.2210/pdb6r0c/pdb
• EMDBエントリー: 4692
• 分子名称: Histone H3.3, Histone H4, Histone H2A type 1, ... (7 entities in total)
• 機能のキーワード: chromatin, nucleosome, retrovirus, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 199182.45

構造登録者

Pye, V.E.,Wilson, M.D.,Cherepanov, P.,Costa, A. (登録日: 2019-03-12, 公開日: 2019-09-25, 最終更新日: 2024-05-15)

主引用文献

Wilson, M.D.,Renault, L.,Maskell, D.P.,Ghoneim, M.,Pye, V.E.,Nans, A.,Rueda, D.S.,Cherepanov, P.,Costa, A.
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer.
Nat Commun, 10:4189-4189, 2019

PubMed Abstract: Retroviral integrase can efficiently utilise nucleosomes for insertion of the reverse-transcribed viral DNA. In face of the structural constraints imposed by the nucleosomal structure, integrase gains access to the scissile phosphodiester bonds by lifting DNA off the histone octamer at the site of integration. To clarify the mechanism of DNA looping by integrase, we determined a 3.9 Å resolution structure of the prototype foamy virus intasome engaged with a nucleosome core particle. The structural data along with complementary single-molecule Förster resonance energy transfer measurements reveal twisting and sliding of the nucleosomal DNA arm proximal to the integration site. Sliding the nucleosomal DNA by approximately two base pairs along the histone octamer accommodates the necessary DNA lifting from the histone H2A-H2B subunits to allow engagement with the intasome. Thus, retroviral integration into nucleosomes involves the looping-and-sliding mechanism for nucleosomal DNA repositioning, bearing unexpected similarities to chromatin remodelers.

PubMed: 31519882
DOI: 10.1038/s41467-019-12007-w

実験手法

ELECTRON MICROSCOPY (4.2 Å)