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|Title: ||CRL2 aids elimination of truncated selenoproteins produced by failed UGA/Sec decoding|
|Authors: ||Hsiu-Chuan Lin;Szu-Chi Ho;Yi-Yun Chen;Kay-Hooi Khoo;Pang-Hung Hsu;Hsueh-Chi S. Yen|
|Issue Date: ||2018-03-22T02:12:03Z
|Abstract: ||Abstract: Selenocysteine (Sec) is translated from the codon UGA, typically a termination signal. Codon duality extends the genetic code; coexistence of two competing UGA-decoding mechanisms, however, immediately compromises proteome fidelity. Selenium availability tunes reassignment of UGA to Sec. We report a CRL2 ubiquitin ligase-mediated protein quality control system that specifically eliminates truncated proteins consequent of 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.|
|Appears in Collections:||[生命科學系] 期刊論文|
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