ArticleThe EMBO journal2002
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.
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Who cites it
54 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins.Frontiers in bioinformatics · 2026Pooled it
- Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025Article
- An updated overview on the bacterial PhoP/PhoQ two-component signal transduction system.Frontiers in cellular and infection microbiology · 2025Review
- RcsF-independent mechanisms of signaling within the Rcs phosphorelay.PLoS genetics · 2024Article
- RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024Article
- Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin binding.The Journal of biological chemistry · 2024Article
- Development of a sensor for disulfide bond formation in diverse bacteria.Journal of bacteriology · 2024Article
- Distinct enzymatic strategies forCritical reviews in biochemistry and molecular biology · 2023Article
- Identification of a Thiol-Disulfide Oxidoreductase (SdbA) Catalyzing Disulfide Bond Formation in the Superantigen SpeA in Streptococcus pyogenes.Journal of bacteriology · 2021Article
- Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.Plant physiology · 2021Article
- Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.Journal of molecular biology · 2020Review
- Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) inACS omega · 2019Article
- Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes.Molecular microbiology · 2019Article
- Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.Journal of bacteriology · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments.Microbiology (Reading, England) · 2017Article
- The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli.Journal of bacteriology · 2017Article
- Reoxidation of the Thiol-Disulfide Oxidoreductase MdbA by a Bacterial Vitamin K Epoxide Reductase in the Biofilm-Forming Actinobacterium Actinomyces oris.Journal of bacteriology · 2017Article
- Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.The Journal of biological chemistry · 2017Article
- The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain.Molecular microbiology · 2017Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein disulfide bond formation in Escherichia coli is catalyzed by the periplasmic protein DsbA. A cytoplasmic membrane protein DsbB maintains DsbA in the oxidized state by transferring electrons from DsbA to quinones in the respiratory chain. Here we show that DsbB activity can be reconstituted by co-expression of N- and C-terminal fragments of the protein, each containing one of its redox-active disulfide bonds. This system has allowed us (i) to demonstrate that the two DsbB redox centers interact directly through a disulfide bond formed between the two DsbB domains and (ii) to identify the specific cysteine residues involved in this covalent interaction. Moreover, we are able to capture an intermediate in the process of electron transfer from one redox center to the other. These results lead us to propose a model that describes how the cysteines cooperate in the early stages of oxidation of DsbA. DsbB appears to adopt a novel mechanism to oxidize DsbA, using its two pairs of cysteines in a coordinated reaction to accept electrons from the active cysteines in DsbA.
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