ArticleProceedings of the National Academy of Sciences of the United States of America2007
A highly efficient form of the selenocysteine insertion sequence element in protozoan parasites and its use in mammalian cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 73 citations in OpenAlex.
- Targeting the TRIM14/USP14 axis enhances radiotherapy efficacy by inducing GPX4 degradation and disrupting ferroptotic defense in HCC.Cell death & disease · 2025Article
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Development of a sensor to detect methylmercury toxicity.Scientific reports · 2024Article
- Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023Review
- Deciphering the Role of Selenoprotein M.Antioxidants (Basel, Switzerland) · 2023Review
- Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins.Frontiers in molecular biosciences · 2023Article
- Selenium and protozoan parasitic infections: selenocompounds and selenoproteins potential.Parasitology research · 2022Review
- Expression of selenoproteins via genetic code expansion in mammalian cells.Methods in enzymology · 2022Article
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162.Acta crystallographica. Section D, Structural biology · 2021Article
- Generation of Recombinant Mammalian Selenoproteins through Genetic Code Expansion with Photocaged Selenocysteine.ACS chemical biology · 2020Article
- Selective covalent targeting of GPX4 using masked nitrile-oxide electrophiles.Nature chemical biology · 2020Article
- Chemical Biology Approaches to Interrogate the Selenoproteome.Accounts of chemical research · 2019Review
- Improving redox sensitivity of roGFP1 by incorporation of selenocysteine at position 147.BMC research notes · 2018Article
- Stable and Potent Selenomab-Drug Conjugates.Cell chemical biology · 2017Article
- Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depletedThe Journal of biological chemistry · 2017Article
- Intrinsic expression of a multiexon type 3 deiodinase gene controls zebrafish embryo size.Endocrinology · 2014Article
- Selenoprotein S is involved in maintenance and transport of multiprotein complexes.The Biochemical journal · 2014Article
- The insertion Green Monster (iGM) method for expression of multiple exogenous genes in yeast.G3 (Bethesda, Md.) · 2014Article
- Chemically programmed antibodies.Trends in biotechnology · 2014Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
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Abstract
Selenoproteins are an elite group of proteins containing a rare amino acid, selenocysteine (Sec), encoded by the codon, UGA. In eukaryotes, incorporation of Sec requires a Sec insertion sequence (SECIS) element, a stem-loop structure located in the 3'-untranslated regions of selenoprotein mRNAs. Here we report identification of a noncanonical form of SECIS element in Toxoplasma gondii and Neospora canine, single-celled apicomplexan parasites of humans and domestic animals. This SECIS has a GGGA sequence in the SBP2-binding site in place of AUGA previously considered invariant. Using a combination of computational and molecular techniques, we show that Toxoplasma and Neospora possess both canonical and noncanonical SECIS elements. The GGGA-type SECIS element supported Sec insertion in mammalian HEK 293 and NIH 3T3 cells and did so more efficiently than the natural mammalian SECIS elements tested. In addition, mammalian type I and type II SECIS elements mutated into the GGGA forms were functional but manifested decreased Sec insertion efficiency. We carried out computational searches for both AUGA and GGGA forms of SECIS elements in Toxoplasma and detected five selenoprotein genes, including one coding for a previously undescribed selenoprotein, designated SelQ, and two containing the GGGA form of the SECIS element. In contrast, the GGGA-type SECIS elements were not detected in mammals and nematodes. As a practical outcome of the study, we developed pSelExpress1, a vector for convenient expression of selenoproteins in mammalian cells. It contains an SBP2 gene and the most efficient tested SECIS element: an AUGA mutant of the GGGA-type Toxoplasma SelT structure.
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