Beissinger, Martina and Buchner, Johannes (1998) How chaperones fold proteins. BIOLOGICAL CHEMISTRY, 379 (3). pp. 245-259. ISSN 1431-6730, 1437-4315
Full text not available from this repository.Abstract
Chaperones are a functionally related group of proteins assisting protein folding in the cell under physiological and stress conditions. They share the ability to recognize and bind nonnative proteins thus preventing unspecific aggregation. The underlying functional principles of the different chaperone classes are beginning to be understood. A landmark feature of molecular chaperones is the involvement of energy-dependent reactions in the folding process. Nucleotide binding to ATP-dependent chaperones (e.g. GroEL, Hsp70, Hsp90) leads to sometimes large conformational changes in the chaperone which allow to shift between high-and low-affinity states for substrate proteins. Interestingly, the ATPase activity which is the key determinant for functional cycles is tightly regulated by a set of co-chaperones. While for ATP-dependent chaperones binding sites for nucleotide and protein are found in one protein, in the case of ATP-independent chaperones (e. g. sHsps, SecB) the energy-dependent step is performed by another chaperone (Hsp70, SecA). Therefore, the ATP-independent chaperones can be regarded as efficient 'holding' components. Cooperation of different chaperone machineries creates a synergistic network of folding helpers in the cell, which allows to maintain protein homeostasis under conditions nonpermissive for spontaneous folding.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HEAT-SHOCK PROTEINS; ALPHA-B-CRYSTALLIN; GROEL-GROES COMPLEXES; SUBSTRATE-BINDING DOMAINS; ESCHERICHIA-COLI DNAJ; MOLECULAR CHAPERONE; ATP HYDROLYSIS; SECONDARY STRUCTURE; PEPTIDE-BINDING; CONFORMATIONAL CHANGE; GroE; Hsp70; Hsp90; molecular chaperones; protein folding; sHsp |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 07 Nov 2024 09:33 |
| Last Modified: | 07 Nov 2024 09:33 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50029 |
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