ArticleMicrobial cell factories2010
Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli.
Article in Microbial cell factories, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 119 citations in OpenAlex.
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- Production of neutralizing antibody fragment variants in the cytoplasm of E. coli for rapid screening: SARS-CoV-2 a case study.Scientific reports · 2023Article
- A quantitative interpretation of oxidative protein folding activity in Escherichia coli.Microbial cell factories · 2022Article
- Bioactive VEGF-C from E. coli.Scientific reports · 2022Article
- A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.Nature communications · 2022Article
- Current trends in biopharmaceuticals production in Escherichia coli.Biotechnology letters · 2022Review
- Modern venomics-Current insights, novel methods, and future perspectives in biological and applied animal venom research.GigaScience · 2022Article
- DisCoTune: versatile auxiliary plasmids for the production of disulphide-containing proteins and peptides in the E. coli T7 system.Microbial biotechnology · 2021Article
- CyDisCo production of functional recombinant SARS-CoV-2 spike receptor binding domain.Protein science : a publication of the Protein Society · 2021Article
- Different effects of carbohydrate binding modules on the viscoelasticity of nanocellulose gels.Biochemistry and biophysics reports · 2020Article
- Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins.International journal of molecular sciences · 2020Review
- Production of Extracellular Matrix Proteins in the Cytoplasm ofInternational journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe formation of native disulfide bonds is a complex and essential post-translational modification for many proteins. The large scale production of these proteins can be difficult and depends on targeting the protein to a compartment in which disulfide bond formation naturally occurs, usually the endoplasmic reticulum of eukaryotes or the periplasm of prokaryotes. It is currently thought to be impossible to produce large amounts of disulfide bond containing protein in the cytoplasm of wild-type bacteria such as E. coli due to the presence of multiple pathways for their reduction.
resultsHere we show that the introduction of Erv1p, a sulfhydryl oxidase and FAD-dependent catalyst of disulfide bond formation found in the inter membrane space of mitochondria, allows the efficient formation of native disulfide bonds in heterologously expressed proteins in the cytoplasm of E. coli even without the disruption of genes involved in disulfide bond reduction, for example trxB and/or gor. Indeed yields of active disulfide bonded proteins were higher in BL21 (DE3) pLysSRARE, an E. coli strain with the reducing pathways intact, than in the commercial Δgor ΔtrxB strain rosetta-gami upon co-expression of Erv1p.
conclusionsOur results refute the current paradigm in the field that disruption of at least one of the reducing pathways is essential for the efficient production of disulfide bond containing proteins in the cytoplasm of E. coli and open up new possibilities for the use of E. coli as a microbial cell factory.
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