ArticleMolecular microbiology2008
The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
44 citing papers in PubMed.
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Antibiotic potentiation and inhibition of cross-resistance in pathogens associated with cystic fibrosis.eLife · 2026Article
- Distinct enzymatic strategies forCritical reviews in biochemistry and molecular biology · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Article
- Structural characterization of PaFkbA: A periplasmic chaperone fromComputational and structural biotechnology journal · 2021Article
- How the assembly and protection of the bacterial cell envelope depend on cysteine residues.The Journal of biological chemistry · 2020Review
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Complex Oxidation of ApocytochromesApplied and environmental microbiology · 2019Article
- Disulfide Chaperone Knockouts Enable In Vivo Double Spin Labeling of an Outer Membrane Transporter.Biophysical journal · 2019Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Bacterial Periplasmic Oxidoreductases Control the Activity of Oxidized Human Antimicrobial β-Defensin 1.Infection and immunity · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Changes in the phosphoproteome of brown adipose tissue during hibernation in the ground squirrel,Physiological genomics · 2017Article
- Oxidative stress, protein damage and repair in bacteria.Nature reviews. Microbiology · 2017Review
- Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.Nature · 2015Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Mapping native disulfide bonds at a proteome scale.Nature methods · 2015Article
- Wheat germ in vitro translation to produce one of the most toxic sodium channel specific toxins.Bioscience reports · 2014Article
- A new role for Escherichia coli DsbC protein in protection against oxidative stress.The Journal of biological chemistry · 2014Article
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Authors and funding
9 authors.
Funding
Abstract
In Escherichia coli, DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by DsbB, which generates disulphides from quinone reduction. DsbA is not known to have any proofreading activity and can form incorrect disulphides in proteins with multiple cysteines. These incorrect disulphides are thought to be corrected by a protein disulphide isomerase, DsbC, which is kept in the reduced and active configuration by DsbD. The DsbC/DsbD isomerization pathway is considered to be isolated from the DsbA/DsbB pathway. We show that the DsbC and DsbA pathways are more intimately connected than previously thought. dsbA(-)dsbC(-) mutants have a number of phenotypes not exhibited by either dsbA(-), dsbC(-) or dsbA(-)dsbD(-) mutations: they exhibit an increased permeability of the outer membrane, are resistant to the lambdoid phage Phi80, and are unable to assemble the maltoporin LamB. Using differential two-dimensional liquid chromatographic tandem mass spectrometry/mass spectrometry analysis, we estimated the abundance of about 130 secreted proteins in various dsb(-) strains. dsbA(-)dsbC(-) mutants exhibit unique changes at the protein level that are not exhibited by dsbA(-)dsbD(-) mutants. Our data indicate that DsbC can assist DsbA in a DsbD-independent manner to oxidatively fold envelope proteins. The view that DsbC's function is limited to the disulphide isomerization pathway should therefore be reinterpreted.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.