ArticleMolecular and cellular biology1997
An RNA-binding protein recognizes a mammalian selenocysteine insertion sequence element required for cotranslational incorporation of selenocysteine.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 82 citations in OpenAlex.
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Enhancing Gpx1 palmitoylation to inhibit angiogenesis by targeting PPT1.Redox biology · 2024Article
- Epitranscriptomic systems regulate the translation of reactive oxygen species detoxifying and disease linked selenoproteins.Free radical biology & medicine · 2019Review
- Processive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequence.The Journal of biological chemistry · 2018Article
- Improving redox sensitivity of roGFP1 by incorporation of selenocysteine at position 147.BMC research notes · 2018Article
- Molecular mechanism of selenoprotein P synthesis.Biochimica et biophysica acta. General subjects · 2018Review
- Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB.Nucleic acids research · 2015Article
- Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.RNA biology · 2014Article
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
- Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.Journal of molecular biology · 2013Article
- Identification of nucleotides and amino acids that mediate the interaction between ribosomal protein L30 and the SECIS element.BMC molecular biology · 2013Article
- Selenoprotein N in skeletal muscle: from diseases to function.Journal of molecular medicine (Berlin, Germany) · 2012Review
- Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities.Antioxidants & redox signaling · 2011Review
- Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression.Nucleic acids research · 2010Article
- Threading the needle: getting selenocysteine into proteins.Antioxidants & redox signaling · 2010Review
- Targeting selenium metabolism and selenoproteins: novel avenues for drug discovery.Metallomics : integrated biometal science · 2010Review
- Crystal structure of human selenocysteine tRNA.Nucleic acids research · 2009Article
- Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine.Nucleic acids research · 2009Article
- Regulation of the extracellular antioxidant selenoprotein plasma glutathione peroxidase (GPx-3) in mammalian cells.Molecular and cellular biochemistry · 2009Article
- Functional analysis of the interplay between translation termination, selenocysteine codon context, and selenocysteine insertion sequence-binding protein 2.The Journal of biological chemistry · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In mammalian selenoprotein mRNAs, the recognition of UGA as selenocysteine requires selenocysteine insertion sequence (SECIS) elements that are contained in a stable stem-loop structure in the 3' untranslated region (UTR). In this study, we investigated the SECIS elements and cellular proteins required for selenocysteine insertion in rat phospholipid hydroperoxide glutathione peroxidase (PhGPx). We developed a translational readthrough assay for selenoprotein biosynthesis by using the gene for luciferase as a reporter. Insertion of a UGA or UAA codon into the coding region of luciferase abolished luciferase activity. However, activity was restored to the UGA mutant, but not to the UAA mutant, upon insertion of the PhGPx 3' UTR. The 3' UTR of rat glutathione peroxidase (GPx) also allowed translational readthrough, whereas the PhGPx and GPx antisense 3' UTRs did not. Deletion of two conserved SECIS elements in the PhGPx 3' UTR (AUGA in the 5' stem or AAAAC in the terminal loop) abolished readthrough activity. UV cross-linking studies identified a 120-kDa protein in rat testis that binds specifically to the sense strands of the PhGPx and GPx 3' UTRs. Direct cross-linking and competition experiments with deletion mutant RNAs demonstrated that binding of the 120-kDa protein requires the AUGA SECIS element but not AAAAC. Point mutations in the AUGA motif that abolished protein binding also prevented readthrough of the UGA codon. Our results suggest that the 120-kDa protein is a significant component of the mechanism of selenocysteine incorporation in mammalian cells.
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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.