Item type |
文献 / Documents(1) |
公開日 |
2022-01-04 |
アクセス権 |
|
|
アクセス権 |
open access |
資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
出版社版DOI |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1016/j.isci.2021.102145 |
|
|
言語 |
ja |
|
|
関連名称 |
10.1016/j.isci.2021.102145 |
出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
タイトル |
|
|
タイトル |
The ubiquitination-deubiquitination cycle on the ribosomal protein eS7A is crucial for efficient translation |
|
言語 |
en |
著者 |
タケハラ
ヤシロダ, ヒデキ
マツオ, ヨシタカ
Zhao, Xian
カミガキ, アカネ
マツザキ, テツオ
小迫, 英尊
イナダ, トシフミ
ムラタ, シゲオ
|
抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
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. |
|
言語 |
en |
書誌情報 |
en : iScience
巻 24,
号 3,
p. 102145,
発行日 2021-03-19
|
収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
25890042 |
出版者 |
|
|
出版者 |
Elsevier |
|
言語 |
en |
権利情報 |
|
|
言語 |
en |
|
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/). |
EID |
|
|
識別子 |
376498 |
|
識別子タイプ |
URI |
言語 |
|
|
言語 |
eng |