6I7O
The structure of a di-ribosome (disome) as a unit for RQC and NGD quality control pathways recognition.
これはPDB形式変換不可エントリーです。
6I7O の概要
エントリーDOI | 10.2210/pdb6i7o/pdb |
EMDBエントリー | 4427 |
分子名称 | 25S ribosomal RNA, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (85 entities in total) |
機能のキーワード | ribosome, disome, di-ribosome, stalling, translation |
由来する生物種 | Saccharomyces cerevisiae 詳細 |
タンパク質・核酸の鎖数 | 163 |
化学式量合計 | 6232473.68 |
構造登録者 | |
主引用文献 | Ikeuchi, K.,Tesina, P.,Matsuo, Y.,Sugiyama, T.,Cheng, J.,Saeki, Y.,Tanaka, K.,Becker, T.,Beckmann, R.,Inada, T. Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways. EMBO J., 38:-, 2019 Cited by PubMed Abstract: Ribosome stalling triggers quality control pathways targeting the mRNA (NGD: no-go decay) and the nascent polypeptide (RQC: ribosome-associated quality control). RQC requires Hel2-dependent uS10 ubiquitination and the RQT complex in yeast. Here, we report that Hel2-dependent uS10 ubiquitination and Slh1/Rqt2 are crucial for RQC and NGD induction within a di-ribosome (disome) unit, which consists of the leading stalled ribosome and the following colliding ribosome. Hel2 preferentially ubiquitinated a disome over a monosome on a quality control inducing reporter mRNA in an translation reaction. Cryo-EM analysis of the disome unit revealed a distinct structural arrangement suitable for recognition and modification by Hel2. The absence of the RQT complex or uS10 ubiquitination resulted in the elimination of NGD within the disome unit. Instead, we observed Hel2-mediated cleavages upstream of the disome, governed by initial Not4-mediated monoubiquitination of eS7 and followed by Hel2-mediated K63-linked polyubiquitination. We propose that Hel2-mediated ribosome ubiquitination is required both for canonical NGD (NGD) and RQC coupled to the disome and that RQC-uncoupled NGD outside the disome (NGD) can occur in a Not4-dependent manner. PubMed: 30609991DOI: 10.15252/embj.2018100276 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (5.3 Å) |
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