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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45500

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
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2016
Issue Date: 2018-03-22T02:12:03Z
Publisher: Science
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.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45500
Appears in Collections:[生命科學系] 期刊論文

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