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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Khoo, Kay-hooi Hsu, Pang-hung Lin, Hsiu-chuan Ho, Szu-chi Yen, Hsueh-chi S. Chen, Yi-yun |
| Description | Author Affiliation: Lin HC ( Institute of Molecular Biology, Academia Sinica, Taiwan. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan.); Ho SC ( Institute of Molecular Biology, Academia Sinica, Taiwan.); Chen YY ( Institute of Biological Chemistry, Academia Sinica, Taiwan.); Khoo KH ( Genome and Systems Biology Degree Program, National Taiwan University, Taiwan. Institute of Biological Chemistry, Academia Sinica, Taiwan.); Hsu PH ( Department of Life Science, Institute of Bioscience and Biotechnology, National Taiwan Ocean University, Taiwan.); Yen HC ( Institute of Molecular Biology, Academia Sinica, Taiwan. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan.) |
| Abstract | 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. |
| ISSN | 00368075 |
| e-ISSN | 10959203 |
| Journal | Science |
| Issue Number | 6243 |
| Volume Number | 349 |
| Language | English |
| Publisher | American Association for the Advancement of Science (United States) |
| Publisher Date | 2015-07-03 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Peptide Chain Termination, Translational Genetics Proteolysis SKP Cullin F-Box Protein Ligases Metabolism Selenocysteine Selenoproteins Codon, Terminator HEK293 Cells Selenium Ubiquitin Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | History and Philosophy of Science |
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