ArticleProceedings of the National Academy of Sciences of the United States of America1998
The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 85 citations in OpenAlex.
- Glycolytic reprograming in Salmonella counters NOX2-mediated dissipation of ΔpH.Nature communications · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Comparative proteome analysis in an Escherichia coli CyDisCo strain identifies stress responses related to protein production, oxidative stress and accumulation of misfolded protein.Microbial cell factories · 2019Article
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Disulfide bond formation in prokaryotes: history, diversity and design.Biochimica et biophysica acta · 2014Review
- Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.PloS one · 2014Article
- Cloning of Soluble Human Stem Cell Factor in pET-26b(+) Vector.Advanced pharmaceutical bulletin · 2014Article
- Article
- Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.Molecular microbiology · 2012Article
- Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach.PLoS computational biology · 2012Article
- Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.Chemical reviews · 2011Review
- Single-gene deletion mutants of Escherichia coli with altered sensitivity to bicyclomycin, an inhibitor of transcription termination factor Rho.Journal of bacteriology · 2011Article
- Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.Biochemistry · 2010Article
- Mechanisms of oxidative protein folding in the bacterial cell envelope.Antioxidants & redox signaling · 2010Review
- Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization.BMC microbiology · 2010Article
- Antibiotic sensitivity profiles determined with an Escherichia coli gene knockout collection: generating an antibiotic bar code.Antimicrobial agents and chemotherapy · 2010Article
- Identification of candidates for cyclotide biosynthesis and cyclisation by expressed sequence tag analysis of Oldenlandia affinis.BMC genomics · 2010Article
- Expression, purification and molecular structure modeling of thioredoxin (Trx) and thioredoxin reductase (TrxR) from Acidithiobacillus ferrooxidans.Current microbiology · 2009Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Thioredoxin 1 is a major thiol-disulfide oxidoreductase in the cytoplasm of Escherichia coli. One of its functions is presumed to be the reduction of the disulfide bond in the active site of the essential enzyme ribonucleotide reductase. Thioredoxin 1 is kept in a reduced state by thioredoxin reductase. In a thioredoxin reductase null mutant however, most of thioredoxin 1 is in the oxidized form; recent reports have suggested that this oxidized form might promote disulfide bond formation in vivo. In the Escherichia coli periplasm, the protein disulfide isomerase DsbC is maintained in the reduced and active state by the membrane protein DsbD. In a dsbD null mutant, DsbC accumulates in the oxidized form. This oxidized form is then able to promote disulfide bond formation. In both these cases, the inversion of the function of these thiol oxidoreductases appears to be due to an altered redox balance of the environment in which they find themselves. Here, we show that thioredoxin 1 attached to the alkaline phosphatase signal sequence can be exported into the E. coli periplasm. In this new environment for thioredoxin 1, we show that thioredoxin 1 can promote disulfide bond formation and, therefore, partially complement a dsbA strain defective for disulfide bond formation. Thus, we provide evidence that by changing the location of thioredoxin 1 from cytoplasm to periplasm, we change its function from a reductant to an oxidant. We conclude that the in vivo redox function of thioredoxin 1 depends on the redox environment in which it is localized.
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