The ubiquitination-deubiquitination cycle on the ribosomal protein eS7A is crucial for efficient translation

iScience

Shigeo Murata¹  Hidetaka Kosako²  Toshifumi Inada³  Yoshitaka Matsuo³  Yuka Takehara⁴  Tetsuo Matsuzaki⁴  Hideki Yashiroda⁴  Akane Kamigaki⁴  Xian Zhao⁴ 

[1] Department of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639, Japan;Division of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, 3-18-15 Kuramoto-cho, Tokushima 770-8503, Japan;Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba-ku, Sendai 980-8578, Japan;Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan;

关键词: biological sciences;    biochemistry;    molecular biology;   

DOI  :  

来源: DOAJ

【 摘 要 】

Summary: 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.

【 授权许可】

Unknown