ArticleThe Journal of biological chemistry2007
Functional analysis of the interplay between translation termination, selenocysteine codon context, and selenocysteine insertion sequence-binding protein 2.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Exogenous Selenoprotein V Induces Apoptosis in Murine Testicular Teratoma Cells via Mitochondrial Dysfunction and ROS Overproduction.Biomolecules · 2025Article
- Selenium, Stroke, and Infection: A Threefold Relationship; Where Do We Stand and Where Do We Go?Nutrients · 2023Review
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- The Interaction between Dietary Selenium Intake and Genetics in Determining Cancer Risk and Outcome.Nutrients · 2020Review
- Processive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequence.The Journal of biological chemistry · 2018Article
- The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine Incorporation.Journal of molecular biology · 2018Article
- Molecular mechanism of selenoprotein P synthesis.Biochimica et biophysica acta. General subjects · 2018Review
- Review
- Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.The Journal of biological chemistry · 2014Article
- Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities.Antioxidants & redox signaling · 2011Review
- Firefly luciferase and RLuc8 exhibit differential sensitivity to oxidative stress in apoptotic cells.PloS one · 2011Article
- The efficiency of selenocysteine incorporation is regulated by translation initiation factors.Journal of molecular biology · 2010Article
- Processive selenocysteine incorporation during synthesis of eukaryotic selenoproteins.Journal of molecular biology · 2010Article
- Threading the needle: getting selenocysteine into proteins.Antioxidants & redox signaling · 2010Review
- Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors.Cellular and molecular life sciences : CMLS · 2010Review
- Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine.Nucleic acids research · 2009Article
- Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling.Endocrine reviews · 2008Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
A selenocysteine insertion sequence (SECIS) element in the 3'-untranslated region and an in-frame UGA codon are the requisite cis-acting elements for the incorporation of selenocysteine into selenoproteins. Equally important are the trans-acting factors SBP2, Sec-tRNA[Ser]Sec, and eEFSec. Multiple in-frame UGAs and two SECIS elements make the mRNA encoding selenoprotein P (Sel P) unique. To study the role of codon context in determining the efficiency of UGA readthrough at each of the 10 rat Sel P Sec codons, we individually cloned 27-nucleotide-long fragments representing each UGA codon context into a luciferase reporter construct harboring both Sel P SECIS elements. Significant differences, spanning an 8-fold range of UGA readthrough efficiency, were observed, but these differences were dramatically reduced in the presence of excess SBP2. Mutational analysis of the "fourth base" of contexts 1 and 5 revealed that only the latter followed the established rules for hierarchy of translation termination. In addition, mutations in either or both of the Sel P SECIS elements resulted in differential effects on UGA readthrough. Interestingly, even when both SECIS elements harbored a mutation of the core region required for Sec incorporation, context 5 retained a significantly higher level of readthrough than context 1. We also show that SBP2-dependent Sec incorporation is able to repress G418-induced UGA readthrough as well as eRF1-induced stimulation of termination. We conclude that a large codon context forms a cis-element that works together with Sec incorporation factors to determine readthrough efficiency.
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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.