ArticleJournal of molecular biology2010
The efficiency of selenocysteine incorporation is regulated by translation initiation factors.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- The Combinatorial Fusion Cascade to Generate the Standard Genetic Code.Life (Basel, Switzerland) · 2021Article
- Selenium in Human Health and Gut Microflora: Bioavailability of Selenocompounds and Relationship With Diseases.Frontiers in nutrition · 2021Review
- Combinatorial Fusion Rules to Describe Codon Assignment in the Standard Genetic Code.Life (Basel, Switzerland) · 2020Article
- Selenium and Selenoproteins in Adipose Tissue Physiology and Obesity.Biomolecules · 2020Review
- Multiple RNA structures affect translation initiation and UGA redefinition efficiency during synthesis of selenoprotein P.Nucleic acids research · 2017Article
- Human selenoprotein P and S variant mRNAs with different numbers of SECIS elements and inferences from mutant mice of the roles of multiple SECIS elements.Open biology · 2016Article
- Hypermethylated-capped selenoprotein mRNAs in mammals.Nucleic acids research · 2014Article
- Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.RNA biology · 2014Article
- Effects of selenoprotein S on oxidative injury in human endothelial cells.Journal of translational medicine · 2013Article
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
- Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.Journal of molecular biology · 2013Article
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Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Selenocysteine (Sec) incorporation is an essential process required for the production of at least 25 human selenoproteins. This unique amino acid is co-translationally incorporated at specific UGA codons that normally serve as termination signals. Recoding from stop to Sec involves a cis-acting Sec insertion sequence element in the 3' untranslated region of selenoprotein mRNAs as well as Sec insertion sequence binding protein 2, Sec-tRNA(Sec), and the Sec-specific elongation factor, eEFSec. The interplay between recoding and termination at Sec codons has served as a focal point in researching the mechanism of Sec insertion, but the role of translation initiation has not been addressed. In this report, we show that the cricket paralysis virus intergenic internal ribosome entry site is able to support Sec incorporation, thus providing evidence that the canonical functions of translation initiation factors are not required. Additionally, we show that neither a 5' cap nor a 3' poly(A) tail enhances Sec incorporation. Interestingly, however, the presence of the internal ribosome entry site significantly decreases Sec incorporation efficiency, suggesting a role for translation initiation in regulating the efficiency of UGA recoding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.