ArticleMolecular microbiology2012
Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- A phase-separated CO2-fixing pyrenoid proteome determined by TurboID in Chlamydomonas reinhardtii.The Plant cell · 2023Article
- Rhodaneses minimize the accumulation of cellular sulfane sulfur to avoid disulfide stress during sulfide oxidation in bacteria.Redox biology · 2022Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Deletion of BmoR affects the expression of genes related to thiol/disulfide balance in Bacteroides fragilis.Scientific reports · 2018Article
- Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.Journal of bacteriology · 2018Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli.Journal of bacteriology · 2017Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain.Molecular microbiology · 2017Article
- Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria.Nature chemical biology · 2015Article
- 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
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7 authors at 4 institutions in 4 countries.
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Abstract
Escherichia coli uses the DsbA/DsbB system for introducing disulphide bonds into proteins in the cell envelope. Deleting either dsbA or dsbB or both reduces disulphide bond formation but does not entirely eliminate it. Whether such background disulphide bond forming activity is enzyme-catalysed is not known. To identify possible cellular factors that might contribute to the background activity, we studied the effects of overexpressing endogenous proteins on disulphide bond formation in the periplasm. We find that overexpressing PspE, a periplasmic rhodanese, partially restores substantial disulphide bond formation to a dsbA strain. This activity depends on DsbC, the bacterial disulphide bond isomerase, but not on DsbB. We show that overexpressed PspE is oxidized to the sulphenic acid form and reacts with substrate proteins to form mixed disulphide adducts. DsbC either prevents the formation of these mixed disulphides or resolves these adducts subsequently. In the process, DsbC itself gets oxidized and proceeds to catalyse disulphide bond formation. Although this PspE/DsbC system is not responsible for the background disulphide bond forming activity, we suggest that it might be utilized in other organisms lacking the DsbA/DsbB system.
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