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• W2104611484 endingPage "2412" @default.
• W2104611484 startingPage "2405" @default.
• W2104611484 abstract "One of the proposed roles of the GroEL-GroES cavity is to provide an infinite dilution folding chamber where protein substrate can fold avoiding deleterious off-pathway aggregation. Support for this hypothesis has been strengthened by a number of studies that demonstrated a mandatory GroES requirement under nonpermissive solution conditions, i.e., the conditions where proteins cannot spontaneously fold. We have found that the refolding of glutamine synthetase (GS) does not follow this pattern. In the presence of natural osmolytes trimethylamine N-oxide (TMAO) or potassium glutamate, refolding GS monomers readily aggregate into very large inactive complexes and fail to reactivate even at low protein concentration. Surprisingly, under these nonpermissive folding conditions, GS can reactivate with GroEL and ATP alone and does not require the encapsulation by GroES. In contrast, the chaperonin dependent reactivation of GS under another nonpermissive condition of low Mg2+ (<2 mM MgCl2) shows an absolute requirement of GroES. High-performance liquid chromatography gel filtration analysis and irreversible misfolding kinetics show that a major species of the GS folding intermediates, generated under these low Mg2+ conditions exist as long-lived metastable monomers that can be reactivated after a significantly delayed addition of the GroEL. Our results indicate that the GroES requirement for refolding of GS is not simply dictated by the aggregation propensity of this protein substrate. Our data also suggest that the GroEL-GroES encapsulated environment is not required under all nonpermissive folding conditions." @default.
• W2104611484 created "2016-06-24" @default.
• W2104611484 creator A5001974475 @default.
• W2104611484 creator A5055232045 @default.
• W2104611484 date "2000-01-01" @default.
• W2104611484 modified "2023-10-12" @default.
• W2104611484 title "Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: Off-pathway aggregation propensity does not determine the co-chaperonin requirement" @default.
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• W2104611484 doi "https://doi.org/10.1110/ps.9.12.2405" @default.
• W2104611484 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2144532" @default.
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