8B3G

C(N)RL4CSA-UVSSA-E2-ubiquitin complex.

8B3G の概要

• エントリーDOI: 10.2210/pdb8b3g/pdb
• EMDBエントリー: 15827
• 分子名称: ubiquitin-conjugating enzyme E2 D2 isoform X3, NEDD8, E3 ubiquitin-protein ligase RBX1, ... (9 entities in total)
• 機能のキーワード: transcription, dna repair, ubiquitin, cryo-em
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 386132.85

構造登録者

Kokic, G.,Cramer, P. (登録日: 2022-09-16, 公開日: 2024-09-04, 最終更新日: 2025-07-09)

主引用文献

Kokic, G.,Yakoub, G.,van den Heuvel, D.,Wondergem, A.P.,van der Meer, P.J.,van der Weegen, Y.,Chernev, A.,Fianu, I.,Fokkens, T.J.,Lorenz, S.,Urlaub, H.,Cramer, P.,Luijsterburg, M.S.
Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair.
Nat.Struct.Mol.Biol., 31:536-547, 2024

PubMed Abstract: 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.

PubMed: 38316879
DOI: 10.1038/s41594-023-01207-0

実験手法

ELECTRON MICROSCOPY (4.4 Å)