Homeostatic regulation of ribosomal proteins by ubiquitin-independent cotranslational degradation

6Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Ribosomes are the workplace for protein biosynthesis. Protein production required for normal cell function is tightly linked to ribosome abundance. It is well known that ribosomal genes are actively transcribed and ribosomal messenger RNAs (mRNAs) are rapidly translated, and yet ribosomal proteins have relatively long half-lives. These observations raise questions as to how homeostasis of ribosomal proteins is controlled. Here, we show that ribosomal proteins, while posttranslationally stable, are subject to high-level cotranslational protein degradation (CTPD) except for those synthesized as ubiquitin (Ub) fusion precursors. The N-terminal Ub moiety protects fused ribosomal proteins from CTPD. We further demonstrate that cotranslational folding efficiency and expression level are two critical factors determining CTPD of ribosomal proteins. Different from canonical posttranslational degradation, we found that CTPD of all the ribosomal proteins tested in this study does not require prior ubiquitylation. This work provides insights into the regulation of ribosomal protein homeostasis and furthers our understanding of the mechanism and biological significance of CTPD.

Cite

CITATION STYLE

APA

Ju, D., Li, L., & Xie, Y. (2023). Homeostatic regulation of ribosomal proteins by ubiquitin-independent cotranslational degradation. Proceedings of the National Academy of Sciences of the United States of America, 120(30). https://doi.org/10.1073/pnas.2306152120

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free