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The Essential Function of Protein-disulfide Isomerase Is to Unscramble Non-native Disulfide Bonds
Open accessAbstract
Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC. Haploid pdi1 delta Saccharomyces cerevisiae are inviable, but can be complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI (shufflease). In contrast, pdi1 delta yeast cannot be complemented with a gene coding for SGHC PDI. In vitro, shufflease is an efficient catalyst for the isomerization of existing disulfide bonds but not for dithiol oxidation or disulfide bond reduction. SGHC PDI catalyzes none of these processes. These results indicate that in vivo protein folding pathways contain intermediates with non-native disulfide bonds, and that the essential role of PDI is to unscramble these intermediates.
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Citations
Cited by
Oxidative protein folding in eukaryotes
Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, D. T. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 615
The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum
Frand, A. R., & Kaiser, C. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80017-9 · Cited by 494
Pizarro-Cerdá, J., Méresse, S., Parton, R. G., van der Goot, G., Sola-Landa, A., Lopez-Goñi, I., Moreno, E., & Gorvel, J.-P. (1998) · Infection and Immunity · doi:10.1128/iai.66.12.5711-5724.1998 · Cited by 423
Shusta, E. V., Raines, R. T., Plückthun, A., & Wittrup, K. D. (1998) · Nature Biotechnology · doi:10.1038/nbt0898-773 · Cited by 276
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Metadata
- Authors
- Laboissière, M. C. A., Sturley, S. L., & Raines, R. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-11
- Volume
- 270
- Issue
- 47
- Pages
- 28006-28009
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2071197084
- Cited by
- 210
- References
- 0
- FWCI
- 3.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Laboissière, M. C. A., Sturley, S. L., & Raines, R. T. (1995). The Essential Function of Protein-disulfide Isomerase Is to Unscramble Non-native Disulfide Bonds. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.47.28006
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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