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Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds.
Open accessAbstract
D-Glyceraldehyde-3-phosphate dehydrogenase (GAP-DH) is a protein containing no disulfide bonds; the guanidine HCl-denatured enzyme shows only a limited extent of refolding and reactivation upon dilution, and the enzyme is particularly prone to aggregation during the dilution process. With increasing GAPDH concentration, reactivation decreases and aggregation increases. The presence of protein disulfide isomerase in the dilution mixture markedly increases reactivation of GAPDH and at the same time prevents the aggregation of GAPDH as shown by light-scattering measurements. It is suggested that upon dilution, denatured GAPDH is faced with two competing processes of correct folding and assembly to yield the native enzyme and non-productive association of the partially refolded species to form aggregates. Independent of the isomerase activity as no disulfide bond is present in GAPDH, protein disulfide isomerase assists the refolding of GAPDH to its active state by suppressing aggregation in a way closely similar to the action of chaperones.
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Cited by
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
Gauss, R., Kanehara, K., Carvalho, P., Ng, D. T. W., & Aebi, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.027 · Cited by 124
Mohan, C., Park, S. H., Chung, J. Y., & Lee, G. M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21453 · Cited by 73
Moen, K. E., & Moreno, S. N. J. (2026) · mBio · doi:10.1128/mbio.03124-25
Metadata
- Authors
- Cai, H., Wang, C. C., & Tsou, C. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-10
- Volume
- 269
- Issue
- 40
- Pages
- 24550-24552
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1559988816
- Cited by
- 277
- References
- 0
- FWCI
- 3.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Cai, H., Wang, C. C., & Tsou, C. L. (1994). Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)31426-6
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