ArticleNucleic acids research2005
Selenocysteine insertion directed by the 3'-UTR SECIS element in Escherichia coli.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Design of synthetic selenopeptides with antioxidant activity for the treatment of XP and non-melanoma skin cancer.Frontiers in systems biology · 2026Article
- Selenium and selenoproteins: key regulators of ferroptosis and therapeutic targets in cancer.Journal of molecular medicine (Berlin, Germany) · 2025Review
- Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Selenoproteins and tRNA-Sec: regulators of cancer redox homeostasis.Trends in cancer · 2023Review
- Why Selenocysteine Is Unique?Frontiers in molecular biosciences · 2020Article
- Molecular dynamics-derived rotamer libraries for d-amino acids within homochiral and heterochiral polypeptides.Protein engineering, design & selection : PEDS · 2018Article
- The Anti-Oxidant Defense System of the Marine Polar Ciliate Euplotes nobilii: Characterization of the MsrB Gene Family.Biology · 2017Article
- Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins.Organic & biomolecular chemistry · 2016Article
- Selenium utilization in thioredoxin and catalytic advantage provided by selenocysteine.Biochemical and biophysical research communications · 2015Article
- Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein augmenter of liver regeneration.Archives of biochemistry and biophysics · 2014Article
- (77)Se enrichment of proteins expands the biological NMR toolbox.Journal of molecular biology · 2013Article
- Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.Molecular microbiology · 2011Article
- Expressed protein ligation for metalloprotein design and engineering.Methods in enzymology · 2009Article
- New strategies for the isolation and activity determination of naturally occurring type-4 glutathione peroxidase.Protein expression and purification · 2008Article
- A highly efficient form of the selenocysteine insertion sequence element in protozoan parasites and its use in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Co-translational insertion of selenocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion sequence (SECIS) elements. In known bacterial selenoprotein genes, SECIS elements are located in the coding regions immediately downstream of UGA codons. Here, we report that a distant SECIS element can also function in Sec insertion in bacteria provided that it is spatially close to the UGA codon. We expressed a mammalian phospholipid hydroperoxide glutathione peroxidase in Escherichia coli from a construct in which a natural E.coli SECIS element was located in the 3'-untranslated region (3'-UTR) and adjacent to a sequence complementary to the region downstream of the Sec UGA codon. Although the major readthrough event at the UGA codon was insertion of tryptophan, Sec was also incorporated and its insertion was dependent on the functional SECIS element in the UTR, base-pairing potential of the SECIS flanking region and the Sec UGA codon. These data provide important implications into evolution of SECIS elements and development of a system for heterologous expression of selenoproteins and show that in addition to the primary sequence arrangement between UGA codons and SECIS elements, their proximity within the tertiary structure can support Sec insertion in bacteria.
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