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Small heat shock proteins are molecular chaperones.
Open accessAbstract
Small heat shock proteins (sHsp) with a molecular mass of 15-30 kDa are ubiquitous and conserved. Up to now their function has remained enigmatic. Increased expression under heat shock conditions and their protective effect on cell viability at elevated temperatures suggest that they may have a function in the formation or maintenance of the native conformation of cytosolic proteins. To test this hypothesis we studied the influence of murine Hsp25, human Hsp27, and bovine alpha-B-crystallin (an eye lens protein homologous to sHsps) on the unfolding and refolding of citrate synthase and alpha-glucosidase in vitro. Here we show that all sHsps investigated act as molecular chaperones in these folding reactions. At stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins. Furthermore, they promote the functional refolding of these proteins after urea denaturation similar to GroE and Hsp90. The interaction both with unfolding and refolding proteins seems to be ATP-independent.
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Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
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Metadata
- Authors
- Jakob, U., Gaestel, M., Engel, K., & Buchner, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-01
- Volume
- 268
- Issue
- 3
- Pages
- 1517-1520
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1537274817
- Cited by
- 1,376
- References
- 1
- FWCI
- 22.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Jakob, U., Gaestel, M., Engel, K., & Buchner, J. (1993). Small heat shock proteins are molecular chaperones. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)53882-5
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
