Publication Date:
2015-07-04
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4766860/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4766860/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Hsiu-Chuan -- Ho, Szu-Chi -- Chen, Yi-Yun -- Khoo, Kay-Hooi -- Hsu, Pang-Hung -- Yen, Hsueh-Chi S -- AG011085/AG/NIA NIH HHS/ -- R01 AG011085/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2015 Jul 3;349(6243):91-5. doi: 10.1126/science.aab0515.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Academia Sinica, Taiwan. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan. ; Institute of Molecular Biology, Academia Sinica, Taiwan. ; Institute of Biological Chemistry, Academia Sinica, Taiwan. ; Genome and Systems Biology Degree Program, National Taiwan University, Taiwan. Institute of Biological Chemistry, Academia Sinica, Taiwan. ; Department of Life Science, Institute of Bioscience and Biotechnology, National Taiwan Ocean University, Taiwan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26138980" target="_blank"〉PubMed〈/a〉
Keywords:
Codon, Terminator
;
HEK293 Cells
;
Humans
;
Peptide Chain Termination, Translational/*genetics
;
*Proteolysis
;
SKP Cullin F-Box Protein Ligases/*metabolism
;
Selenium/metabolism
;
Selenocysteine/genetics/*metabolism
;
Selenoproteins/genetics/*metabolism
;
Ubiquitin/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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