ArticleProceedings of the National Academy of Sciences of the United States of America2004
Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Bacterial suppressor-of-copper-sensitivity proteins exhibit diverse thiol-disulfide oxidoreductase cellular functions.iScience · 2024Article
- The Transcriptome Analysis of Circular RNAs Between the Doxorubicin- Induced Cardiomyocytes and Bone Marrow Mesenchymal Stem Cells- Derived Exosomes Treated Ones.Combinatorial chemistry & high throughput screening · 2024Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Efficient Antibody Assembly in E. coli Periplasm by Disulfide Bond Folding Factor Co-expression and Culture Optimization.Applied biochemistry and biotechnology · 2017Article
- Direct expression of active human tissue inhibitors of metalloproteinases by periplasmic secretion in Escherichia coli.Microbial cell factories · 2017Article
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme.The Biochemical journal · 2015Article
- Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization.Molecular microbiology · 2015Article
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- Disulfide bond formation in prokaryotes: history, diversity and design.Biochimica et biophysica acta · 2014Review
- Structural and functional characterization of ScsC, a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium.Antioxidants & redox signaling · 2013Article
- Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity.Journal of bacteriology · 2013Article
- Disulfide bond formation in the mammalian endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
- Article
- Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.Antioxidants & redox signaling · 2011Article
- Mechanisms of oxidative protein folding in the bacterial cell envelope.Antioxidants & redox signaling · 2010Review
- Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC.The Journal of biological chemistry · 2009Article
- Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Microbial cell factories · 2009Article
- Engineering antibody fragments to fold in the absence of disulfide bonds.Protein science : a publication of the Protein Society · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In the Escherichia coli periplasm, the formation of protein disulfide bonds is catalyzed by DsbA and DsbC. DsbA is a monomer that is maintained in a fully oxidized state by the membrane enzyme DsbB, whereas DsbC is a dimer that is kept reduced by a second membrane protein, DsbD. Although the catalytic regions of DsbA and DsbC are composed of structurally homologous thioredoxin motif domains, DsbA serves only as an oxidase in vivo, whereas DsbC catalyzes disulfide reduction and isomerization and also exhibits significant chaperone activity. To reconcile the distinct catalytic activities of DsbC and DsbA, we constructed a series of chimeras comprising of the dimerization domain of DsbC, with or without the adjacent alpha-helical linker region, fused either to the first, second, third, or fifth residue of intact DsbA or to thioredoxin. The chimeras fully substituted for DsbC in disulfide-bond rearrangement and also were able to restore protein oxidation in a dsbA background. Remarkably, the chimeras could serve as a single catalyst for both disulfide-bond formation and rearrangement, thus reconciling the kinetically competing DsbB-DsbA and DsbD-DsbC pathways. This property appeared to depend on the orientation of the DsbA active-site cysteines with respect to the DsbC dimerization domain. In vitro, the chimeras had high chaperone activity and significant reductase activity but only 15-22% of the disulfide-isomerization activity of DsbC, suggesting that rearrangement of nonnative disulfides may be mediated primarily by cycles of random reduction and reoxidation.
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