7KBF
H1.8 bound nucleosome isolated from metaphase chromosome in Xenopus egg extract (oligo fraction)
7KBF の概要
| エントリーDOI | 10.2210/pdb7kbf/pdb |
| EMDBエントリー | 22790 22791 22792 |
| 分子名称 | Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total) |
| 機能のキーワード | nucleosome, m phase, cell cycle, chromatin, xenopus egg extract, dna binding protein, h1, chromatosome, linker histone |
| 由来する生物種 | Xenopus laevis (African clawed frog) 詳細 |
| タンパク質・核酸の鎖数 | 11 |
| 化学式量合計 | 246913.95 |
| 構造登録者 | |
| 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 Cited by 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: 34478647DOI: 10.1016/j.molcel.2021.08.010 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.42 Å) |
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