التفاصيل البيبلوغرافية
| العنوان: |
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding. |
| المؤلفون: |
Weber, Frank, Keppel, France, Georgopoulos, Costa, Hayer-Hartl, Manajit K., Hartl, F. Ulrich |
| المصدر: |
Nature Structural Biology; Nov98, Vol. 5 Issue 11, p977, 9p |
| مصطلحات موضوعية: |
OLIGOMERS, MOLECULAR chaperones, PROTEIN folding, ESCHERICHIA coli |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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