DsbG, a protein disulfide isomerase with chaperone activity
Open accessAbstract
DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase. DsbG was also shown to interact with refolding intermediates of chemically denatured citrate synthase and prevents their aggregation in vitro. Citrate synthase reactivation experiments in the presence of DsbG suggest that DsbG binds with high affinity to early unstructured protein folding intermediates. DsbG is one of the first periplasmic proteins shown to have general chaperone activity. This ability to chaperone protein folding is likely to increase the effectiveness of DsbG as a protein disulfide isomerase.
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DsbA, DsbC and DsbG may also have chaperone activity that favors recognition and interaction with substrates necessitating disulfide isomerization.
“In addition, DsbA, DsbC and DsbG may also have a chaperone activity that favors the recognition and interaction with substrates necessitating disulfide isomerization [136].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [136]
The Abstract reports that DsbG has chaperone activity and suggests this may increase its effectiveness as a disulfide isomerase. The Discussion also reports chaperone activity for DsbC and suggests that DsbG recognizes and binds folding intermediates. The paper describes DsbA as rapidly oxidizing protein thiols, but does not attribute chaperone activity to DsbA. (LLM, conf=0.88)
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Cited by
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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
Ishikawa, Y., & Bächinger, H. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561944 · Cited by 52 · see citing works
- Authors
- Shao, F., Bader, M. W., Jakob, U., & Bardwell, J. C. A.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Bardwell, James C.A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 18
- Pages
- 13349-13352
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2001702554
- Cited by
- 116
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 3 · 2016: 1 · 2015: 4 · 2014: 9 · 2013: 7 · 2012: 2
- FWCI
- 3.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- protein disulfide isomerase, molecular chaperones, periplasm, Escherichia coli, citrate synthase, luciferase, protein aggregation, protein folding
- MeSH terms
- Bacterial Proteins, Enzyme Activation, Escherichia coli, Oxidation-Reduction, Oxidoreductases, Molecular Chaperones, Protein Disulfide-Isomerases, Escherichia coli Proteins, Periplasmic Proteins
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