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-Structure paper
| タイトル | Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT. |
|---|---|
| ジャーナル・号・ページ | Sci Adv, Vol. 12, Issue 5, Page eaed1952, Year 2026 |
| 掲載日 | 2026年1月30日 |
著者 | Tomoya Kujirai / Haruhiko Ehara / Tomoko Ito / Masami Henmi / Eriko Oya / Takehiko Kobayashi / Shun-Ichi Sekine / Hitoshi Kurumizaka / ![]() |
| PubMed 要旨 | Trimethylation of the histone H3K36 residue (H3K36me3) plays an indispensable role in ensuring transcription fidelity by suppressing undesired cryptic transcription in chromatin. H3K36me3 ...Trimethylation of the histone H3K36 residue (H3K36me3) plays an indispensable role in ensuring transcription fidelity by suppressing undesired cryptic transcription in chromatin. H3K36me3 modification is accomplished by Set2/SETD2 during transcription elongation by the RNA polymerase II elongation complex (EC). Here, we found that Set2-mediated H3K36me3 deposition occurs on the nucleosome reassembling behind the EC. The histone chaperone FACT suppresses H3K36me3 deposition on the downstream nucleosome, thereby ensuring that Set2 targets specifically on the reassembling upstream nucleosome. Cryo-electron microscopy structures of the nucleosome-transcribing EC complexed with Set2 revealed that Set2 is anchored by the Spt6 subunit of the EC to capture both of the H3 N-terminal tails in a stepwise manner during the nucleosome reassembly process. Abrogation of the Set2-EC interaction leads to defective transcription-coupled H3K36me3 deposition. These insights elucidate the structure-based mechanism of transcription-coupled H3K36me3 deposition in chromatin. |
リンク | Sci Adv / PubMed:41604494 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.4 - 4.66 Å |
| 構造データ | EMDB-66103, PDB-9wms: EMDB-66104, PDB-9wmt: EMDB-66105, PDB-9wmu: EMDB-66106, PDB-9wmv: EMDB-66107, PDB-9wmw: |
| 化合物 | ![]() ChemComp-ZN: ![]() ChemComp-MG: ![]() ChemComp-SAH: |
| 由来 |
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キーワード | TRANSCRIPTION / chromatin / nucleosome |
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Komagataella phaffii (菌類)
homo sapiens (ヒト)
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