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-Structure paper
| タイトル | Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 31, Issue 3, Page 536-547, Year 2024 |
| 掲載日 | 2024年2月5日 |
著者 | Goran Kokic / George Yakoub / Diana van den Heuvel / Annelotte P Wondergem / Paula J van der Meer / Yana van der Weegen / Aleksandar Chernev / Isaac Fianu / Thornton J Fokkens / Sonja Lorenz / Henning Urlaub / Patrick Cramer / Martijn S Luijsterburg / ![]() |
| PubMed 要旨 | During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This ...During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This transition requires site-specific ubiquitylation of Pol II by the CRL4 ubiquitin ligase, a process that is facilitated by ELOF1 in an unknown way. Using cryogenic electron microscopy, biochemical assays and cell biology approaches, we found that ELOF1 serves as an adaptor to stably position UVSSA and CRL4 on arrested Pol II, leading to ligase neddylation and activation of Pol II ubiquitylation. In the presence of ELOF1, a transcription factor IIS (TFIIS)-like element in UVSSA gets ordered and extends through the Pol II pore, thus preventing reactivation of Pol II by TFIIS. Our results provide the structural basis for Pol II ubiquitylation and inactivation in TCR. |
リンク | Nat Struct Mol Biol / PubMed:38316879 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 4.4 Å |
| 構造データ | EMDB-15827, PDB-8b3g: |
| 化合物 | ![]() ChemComp-ZN: |
| 由来 |
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キーワード | TRANSCRIPTION / DNA repair / ubiquitin / cryo-EM |
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