Pathways of disulfide bond formation in Escherichia coli
Abstract
Disulfide bond formation is required for the correct folding of many secreted proteins. Cells possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are joined during the folding process. These enzymatic systems are located in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model.
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The Dsb protein system is composed of five members: DsbA, DsbB, DsbC, DsbD and DsbG.
“The Dsb protein system is composed of five members: DsbA, DsbB, DsbC, DsbD, DsbG [135].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [135]
Cites
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968 · see citing works
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
- Authors
- Messens, J., & Collet, J.-F.
- Affiliations
- Vrije Universiteit Brussel (BE)
- de Duve Institute (BE)
- Corresponding author
- Collet, Jean-François
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2006
- Volume
- 38
- Issue
- 7
- Pages
- 1050-1062
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W1988372753
- Cited by
- 174
- References
- 1
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 2 · 2023: 5 · 2022: 7 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 3 · 2017: 10 · 2016: 4 · 2015: 9 · 2014: 12 · 2013: 12 · 2012: 13
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- DIAL (Catholic University of Leuven) (submittedVersion)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- disulfide bond formation, disulfide bond isomerization, Escherichia coli, protein folding, secreted proteins, periplasm, cysteine pairing
- MeSH terms
- Amino Acid Sequence, Animals, Bacterial Proteins, Catalysis, Cysteine, Disulfides, Endoplasmic Reticulum, Escherichia coli, Membrane Proteins, Models, Molecular, Oxidation-Reduction, Protein Conformation, Thioredoxins, Molecular Structure, Protein Folding, Dimerization, Protein Disulfide-Isomerases
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