ArticleApplied and environmental microbiology2004
Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 85 citations in OpenAlex.
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- Screening Novel Furoxan Derivatives as Potential Inhibitors Targeting Thioredoxin Glutathione Reductase ofPharmaceuticals (Basel, Switzerland) · 2025Article
- Characterization and enzymatic function of thioredoxin glutathione reductase in Orientobilharzia turkestanicum isolated from Xizang.BMC veterinary research · 2025Article
- Optimization of an Inclusion Body-Based Production of the Influenza Virus Neuraminidase inBiomolecules · 2022Article
- Capture of carbon dioxide and hydrogen by engineered Escherichia coli: hydrogen-dependent COApplied microbiology and biotechnology · 2021Article
- Synthesis of oxadiazole-2-oxide derivatives as potential drug candidates for schistosomiasis targeting SjTGR.Parasites & vectors · 2021Article
- Glutathione-glutaredoxin is an efficient electron donor system for mammalian p53R2-R1-dependent ribonucleotide reductase.The Journal of biological chemistry · 2019Article
- Activation of TAp73 and inhibition of TrxR by Verteporfin for improved cancer therapy inFuture science OA · 2019Article
- Irreversible inhibition of cytosolic thioredoxin reductase 1 as a mechanistic basis for anticancer therapy.Science translational medicine · 2018Article
- Preparation of Selenocysteine-Containing Forms of Human SELENOK and SELENOS.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depletedThe Journal of biological chemistry · 2017Article
- A novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems.Science advances · 2016Article
- Repurposing auranofin as a lead candidate for treatment of lymphatic filariasis and onchocerciasis.PLoS neglected tropical diseases · 2015Article
- The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death.Cell death & disease · 2015Article
- Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein augmenter of liver regeneration.Archives of biochemistry and biophysics · 2014Article
- Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.The Journal of biological chemistry · 2013Article
- Wobble decoding by the Escherichia coli selenocysteine insertion machinery.Nucleic acids research · 2013Article
- Redox activation of Fe(III)-thiosemicarbazones and Fe(III)-bleomycin by thioredoxin reductase: specificity of enzymatic redox centers and analysis of reactive species formation by ESR spin trapping.Free radical biology & medicine · 2013Article
- The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.Biochemistry · 2013Article
- Multilevel regulation of 2-Cys peroxiredoxin reaction cycle by S-nitrosylation.The Journal of biological chemistry · 2013Article
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Authors and funding
7 authors at 3 institutions in 1 country.
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Abstract
The production of heterologous selenoproteins in Escherichia coli necessitates the design of a secondary structure in the mRNA forming a selenocysteine insertion sequence (SECIS) element compatible with SelB, the elongation factor for selenocysteine insertion at a predefined UGA codon. SelB competes with release factor 2 (RF2) catalyzing translational termination at UGA. Stoichiometry between mRNA, the SelB elongation factor, and RF2 is thereby important, whereas other expression conditions affecting the yield of recombinant selenoproteins have been poorly assessed. Here we expressed the rat selenoprotein thioredoxin reductase, with titrated levels of the selenoprotein mRNA under diverse growth conditions, with or without cotransformation of the accessory bacterial selA, selB, and selC genes. Titration of the selenoprotein mRNA with a pBAD promoter was performed in both TOP10 and BW27783 cells, which unexpectedly could not improve yield or specific activity compared to that achieved in our prior studies. Guided by principal component analysis, we instead discovered that the most efficient bacterial selenoprotein production conditions were obtained with the high-transcription T7lac-driven pET vector system in presence of the selA, selB, and selC genes, with induction of production at late exponential phase. About 40 mg of rat thioredoxin reductase with 50% selenocysteine content could thereby be produced per liter bacterial culture. These findings clearly illustrate the ability of E. coli to upregulate the selenocysteine incorporation machinery on demand and that this is furthermore strongly augmented in late exponential phase. This study also demonstrates that E. coli can indeed be utilized as cell factories for highly efficient production of heterologous selenoproteins such as rat thioredoxin reductase.
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