| Autor: |
Horovitz A; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel; email: Amnon.Horovitz@weizmann.ac.il., Reingewertz TH; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel; email: Amnon.Horovitz@weizmann.ac.il., Cuéllar J; Department of Macromolecular Structure, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain; email: jmv@cnb.csic.es., Valpuesta JM; Department of Macromolecular Structure, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain; email: jmv@cnb.csic.es. |
| Jazyk: |
angličtina |
| Zdroj: |
Annual review of biophysics [Annu Rev Biophys] 2022 May 09; Vol. 51, pp. 115-133. Date of Electronic Publication: 2022 Jan 04. |
| DOI: |
10.1146/annurev-biophys-082521-113418 |
| Abstrakt: |
The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with cavities in which protein (un)folding can take place in a shielding environment. This review focuses on GroEL from Escherichia coli and the eukaryotic chaperonin-containing t-complex polypeptide 1, which differ considerably in their reaction mechanisms despite sharing a similar overall architecture. Although chaperonins feature in many current biochemistry textbooks after being studied intensively for more than three decades, key aspects of their reaction mechanisms remain under debate and are discussed in this review. In particular, it is unclear whether a universal reaction mechanism operates for all substrates and whether it is passive, i.e., aggregation is prevented but the folding pathway is unaltered, or active. It is also unclear how chaperonin clients are distinguished from nonclients and what are the precise roles of the cofactors with which chaperonins interact. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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