期刊
SCIENCE
卷 349, 期 6243, 页码 91-95出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aab0515
关键词
-
资金
- Career Development Award from Academia Sinica [101-CDA-L05]
- Ministry of Science and Technology (MOST) [103-2311-B-001-034-MY3, 102-2113-M-019-003-MY2]
- NIH [AG011085]
Selenocysteine (Sec) is translated from the codon UGA, typically a termination signal. Codon duality extends the genetic code; however, the coexistence of two competing UGA-decoding mechanisms immediately compromises proteome fidelity. Selenium availability tunes the reassignment of UGA to Sec. We report a CRL2 ubiquitin ligase-mediated protein quality-control system that specifically eliminates truncated proteins that result from reassignment failures. Exposing the peptide immediately N-terminal to Sec, a CRL2 recognition degron, promotes protein degradation. Sec incorporation destroys the degron, protecting read-through proteins from detection by CRL2. Our findings reveal a coupling between directed translation termination and proteolysis-assisted protein quality control, as well as a cellular strategy to cope with fluctuations in organismal selenium intake.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据