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-Structure paper
| タイトル | Structural insights into how DEK nucleosome binding facilitates H3K27 trimethylation in chromatin. |
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| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 32, Issue 7, Page 1183-1192, Year 2025 |
| 掲載日 | 2025年2月21日 |
著者 | Tomoya Kujirai / Kenta Echigoya / Yusuke Kishi / Mai Saeki / Tomoko Ito / Junko Kato / Lumi Negishi / Hiroshi Kimura / Hiroshi Masumoto / Yoshimasa Takizawa / Yukiko Gotoh / Hitoshi Kurumizaka / ![]() |
| PubMed 要旨 | Structural diversity of the nucleosome affects chromatin conformations and regulates eukaryotic genome functions. Here we identify DEK, whose function is unknown, as a nucleosome-binding protein. In ...Structural diversity of the nucleosome affects chromatin conformations and regulates eukaryotic genome functions. Here we identify DEK, whose function is unknown, as a nucleosome-binding protein. In embryonic neural progenitor cells, DEK colocalizes with H3 K27 trimethylation (H3K27me3), the facultative heterochromatin mark. DEK stimulates the methyltransferase activity of Polycomb repressive complex 2 (PRC2), which is responsible for H3K27me3 deposition in vitro. Cryo-electron microscopy structures of the DEK-nucleosome complexes reveal that DEK binds the nucleosome by its tripartite DNA-binding mode on the dyad and linker DNAs and interacts with the nucleosomal acidic patch by its newly identified histone-binding region. The DEK-nucleosome interaction mediates linker DNA reorientation and induces chromatin compaction, which may facilitate PRC2 activation. These findings provide mechanistic insights into chromatin structure-mediated gene regulation by DEK. |
リンク | Nat Struct Mol Biol / PubMed:39984731 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.8 - 4.0 Å |
| 構造データ | EMDB-37115, PDB-8kcy: EMDB-37121, PDB-8kd1: EMDB-37149, PDB-8ke0: ![]() EMDB-38443: 193 bp Widom601L nucleosome (closed) ![]() EMDB-38444: 193 bp Widom601L nucleosome (middle) ![]() EMDB-38445: 193 bp Widom601L nucleosome (open) |
| 由来 |
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キーワード | DNA BINDING PROTEIN / Nucleosome / Chromatin / DNA / DEK / Complex / H1.2 |
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