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ID 116543
著者
Takehara, Yuka The University of Tokyo
Yashiroda, Hideki The University of Tokyo
Matsuo, Yoshitaka Tohoku University
Zhao, Xian The University of Tokyo
Kamigaki, Akane The University of Tokyo
Matsuzaki, Tetsuo The University of Tokyo|Nagoya University
Inada, Toshifumi Tohoku University|The University of Tokyo
Murata, Shigeo The University of Tokyo
資料タイプ
学術雑誌論文
抄録
Ubiquitination is a major post-translational modification of ribosomal proteins. The role of ubiquitination in the regulation of ribosome functions is still being elucidated. However, the importance of ribosome deubiquitination remains unclear. Here, we show that the cycle of ubiquitination and deubiquitination of the 40S ribosome subunit eS7 is important for efficient translation. eS7 ubiquitination at lysine 83 is required for efficient protein translation. We identified Otu2 and Ubp3 as the deubiquitinating enzymes for eS7. An otu2Δubp3Δ mutation caused a defect in protein synthesis. Ubp3 inhibited polyubiquitination of eS7 in polysomes to keep eS7 in a mono-ubiquitinated form, whereas Otu2 was specifically bound to the free 40S ribosome and promoted the dissociation of mRNAs from 40S ribosomes in the recycling step. Our results provide clues for understanding the molecular mechanism of the translation system via a ubiquitination-deubiquitination cycle.
掲載誌名
iScience
ISSN
25890042
出版者
Elsevier
24
3
開始ページ
102145
発行日
2021-03-19
権利情報
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
EDB ID
出版社版DOI
出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
出版社版
部局
先端酵素学研究所