The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
GroE facilitates refolding of citrate synthase by suppressing aggregation
Abstract
The molecular chaperone GroE facilitates correct protein folding in vivo and in vitro. The mode of action of GroE was investigated by using refolding of citrate synthase as a model system. In vitro denaturation of this dimeric protein is almost irreversible, since the refolding polypeptide chains aggregate rapidly, as shown directly by a strong, concentration-dependent increase in light scattering. The yields of reactivated citrate synthase were strongly increased upon addition of GroE and MgATP. GroE inhibits aggregation reactions that compete with correct protein folding, as indicated by specific suppression of light scattering. GroEL rapidly forms a complex with unfolded or partially folded citrate synthase molecules. In this complex the refolding protein is protected from aggregation. Addition of GroES and ATP hydrolysis is required to release the polypeptide chain bound to GroEL and to allow further folding to its final, active state.
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Citations
Cites
Principles that Govern the Folding of Protein Chains
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Homologous plant and bacterial proteins chaperone oligomeric protein assembly
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Proteins as molecular chaperones
Ellis, J. (1987) · Nature · doi:10.1038/328378a0 · Cited by 916
Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
Rothman, J. E. (1989) · Cell · doi:10.1016/0092-8674(89)90005-6 · Cited by 879
Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
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Folding and association of proteins
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Self-citationProtein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
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Cited by
Small heat shock proteins are molecular chaperones.
Jakob, U., Gaestel, M., Engel, K., & Buchner, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53882-5 · Cited by 1,376
Self-citationMartin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F.-U. (1991) · Nature · doi:10.1038/352036a0 · Cited by 854
Kiefhaber, T., Rudolph, R., Kohler, H.-H., & Buchner, J. (1991) · Nature Biotechnology · doi:10.1038/nbt0991-825 · Cited by 441
Self-citationProtein folding: local structures, domains, subunits, and assemblies
Jaenicke, R. (1991) · Biochemistry · doi:10.1021/bi00227a001 · Cited by 438
Self-citationFinka, A., Cuendet, A. F. H., Maathuis, F. J. M., Saidi, Y., & Goloubinoff, P. (2012) · The Plant Cell · doi:10.1105/tpc.112.095844 · Cited by 367
Metadata
- Authors
- Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., & Kiefhaber, T.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1991-02-12
- Volume
- 30
- Issue
- 6
- Pages
- 1586-1591
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2006043716
- Cited by
- 485
- References
- 24
- FWCI
- 22.45
- Type
- journal article
- Language
- en
- Open access
- closed
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- Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., & Kiefhaber, T. (1991). GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. https://doi.org/10.1021/bi00220a020
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
