CRL2 aids elimination of truncated selenoproteins produced by failed UGA/Sec decoding

Author:

Lin Hsiu-Chuan12,Ho Szu-Chi1,Chen Yi-Yun3,Khoo Kay-Hooi23,Hsu Pang-Hung4,Yen Hsueh-Chi S.12

Affiliation:

1. Institute of Molecular Biology, Academia Sinica, Taiwan.

2. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan.

3. Institute of Biological Chemistry, Academia Sinica, Taiwan.

4. Department of Life Science, Institute of Bioscience and Biotechnology, National Taiwan Ocean University, Taiwan.

Abstract

Clearing out selenoprotein garbage Our DNA consists of codons that code for 20 different amino acids. Another amino acid, selenocysteine, is also found in several human selenoproteins. Selenocysteine is incorporated through the recoding of a stop codon, but failures in this process result in premature termination of protein synthesis. Lin et al. showed that the potentially dangerous truncated proteins formed in such cases are specifically degraded by a protein quality surveillance system. The surveillance system can specifically recognize the truncated ends of the various prematurely terminated selenoproteins and target their destruction. Science , this issue p. 91

Funder

NIH

Ministry of Science and Technology

MOST

Career Development Award

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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