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-Structure paper
タイトル | Structural Basis of Heterochromatin Formation by Human HP1. |
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ジャーナル・号・ページ | Mol Cell, Vol. 69, Issue 3, Page 385-397.e8, Year 2018 |
掲載日 | 2018年2月1日 |
著者 | Shinichi Machida / Yoshimasa Takizawa / Masakazu Ishimaru / Yukihiko Sugita / Satoshi Sekine / Jun-Ichi Nakayama / Matthias Wolf / Hitoshi Kurumizaka / |
PubMed 要旨 | Heterochromatin plays important roles in transcriptional silencing and genome maintenance by the formation of condensed chromatin structures, which determine the epigenetic status of eukaryotic cells. ...Heterochromatin plays important roles in transcriptional silencing and genome maintenance by the formation of condensed chromatin structures, which determine the epigenetic status of eukaryotic cells. The trimethylation of histone H3 lysine 9 (H3K9me3), a target of heterochromatin protein 1 (HP1), is a hallmark of heterochromatin formation. However, the mechanism by which HP1 folds chromatin-containing H3K9me3 into a higher-order structure has not been elucidated. Here we report the three-dimensional structure of the H3K9me3-containing dinucleosomes complexed with human HP1α, HP1β, and HP1γ, determined by cryogenic electron microscopy with a Volta phase plate. In the structures, two H3K9me3 nucleosomes are bridged by a symmetric HP1 dimer. Surprisingly, the linker DNA between the nucleosomes does not directly interact with HP1, thus allowing nucleosome remodeling by the ATP-utilizing chromatin assembly and remodeling factor (ACF). The structure depicts the fundamental architecture of heterochromatin. |
リンク | Mol Cell / PubMed:29336876 |
手法 | EM (単粒子) |
解像度 | 6.9 - 24.0 Å |
構造データ | EMDB-6738: EMDB-6739: EMDB-6740: EMDB-6835: EMDB-6836: EMDB-6837: |
由来 |
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