PMID:9808043
| Citation |
Weber, F, Keppel, F, Georgopoulos, C, Hayer-Hartl, MK and Hartl, FU (1998) The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding. Nat. Struct. Biol. 5:977-85 |
|---|---|
| Abstract |
Two models are being considered for the mechanism of chaperonin-assisted protein folding in E. coli: (i) GroEL/GroES act primarily by enclosing substrate polypeptide in a folding cage in which aggregation is prevented during folding. (ii) GroEL mediates the repetitive unfolding of misfolded polypeptides, returning them onto a productive folding track. Both models are not mutually exclusive, but studies with the polypeptide-binding domain of GroEL have suggested that unfolding is the primary mechanism, enclosure being unnecessary. Here we investigate the capacity of the isolated apical polypeptide-binding domain to functionally replace the complete GroEL/GroES system. We show that the apical domain binds aggregation-sensitive polypeptides but cannot significantly assist their refolding in vitro and fails to replace the groEL gene or to complement defects of groEL mutants in vivo. A single-ring version of GroEL cannot substitute for GroEL. These results strongly support the view that sequestration of aggregation-prone intermediates in a folding cage is an important element of the chaperonin mechanism. |
| Links |
PubMed Online version:10.1038/2952 |
| Keywords |
Animals; Cattle; Chaperonin 10/chemistry; Chaperonin 10/physiology; Chaperonin 60/chemistry; Chaperonin 60/genetics; Chaperonin 60/physiology; Circular Dichroism; Citrate (si)-Synthase/chemistry; Escherichia coli/chemistry; Genetic Complementation Test; Malate Dehydrogenase/chemistry; Models, Molecular; Protein Conformation; Protein Folding; Recombinant Fusion Proteins; Sequence Deletion; Tetrahydrofolate Dehydrogenase/chemistry; Thiosulfate Sulfurtransferase/chemistry |
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