7KBD

Nucleosome in interphase chromosome formed in Xenopus egg extract (oligo fraction)

7KBD の概要

• エントリーDOI: 10.2210/pdb7kbd/pdb
• EMDBエントリー: 22790
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (6 entities in total)
• 機能のキーワード: nucleosome, interphase, cell cycle, chromatin, dna binding protein, structural protein-dna complex, structural protein/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 204531.34

構造登録者

Arimura, Y.,Funabiki, H. (登録日: 2020-10-02, 公開日: 2021-09-15, 最終更新日: 2024-05-29)

主引用文献

Arimura, Y.,Shih, R.M.,Froom, R.,Funabiki, H.
Structural features of nucleosomes in interphase and metaphase chromosomes.
Mol.Cell, 81:4377-, 2021

PubMed Abstract: Structural heterogeneity of nucleosomes in functional chromosomes is unknown. Here, we devise the template-, reference- and selection-free (TRSF) cryo-EM pipeline to simultaneously reconstruct cryo-EM structures of protein complexes from interphase or metaphase chromosomes. The reconstructed interphase and metaphase nucleosome structures are on average indistinguishable from canonical nucleosome structures, despite DNA sequence heterogeneity, cell-cycle-specific posttranslational modifications, and interacting proteins. Nucleosome structures determined by a decoy-classifying method and structure variability analyses reveal the nucleosome structural variations in linker DNA, histone tails, and nucleosome core particle configurations, suggesting that the opening of linker DNA, which is correlated with H2A C-terminal tail positioning, is suppressed in chromosomes. High-resolution (3.4-3.5 Å) nucleosome structures indicate DNA-sequence-independent stabilization of superhelical locations ±0-1 and ±3.5-4.5. The linker histone H1.8 preferentially binds to metaphase chromatin, from which chromatosome cryo-EM structures with H1.8 at the on-dyad position are reconstituted. This study presents the structural characteristics of nucleosomes in chromosomes.

PubMed: 34478647
DOI: 10.1016/j.molcel.2021.08.010

実験手法

ELECTRON MICROSCOPY (3.38 Å)