PMID:8868484
| Citation |
Ayling, A and Baneyx, F (1996) Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase. Protein Sci. 5:478-87 |
|---|---|
| Abstract |
We have studied the effect of the components of the GroE molecular chaperone machine on the refolding of the Escherichia coli enzyme beta-galactosidase, a tetrameric protein whose 116-kDa promoters should not completely fit within the central cavity of the GroEL toroid. In the absence of other additives, GroEL formed a weak complex with chemically denatured beta-galactosidase, reduced its propensity to aggregate, and increased the recovery yields of active enzyme twofold without altering its folding pathway. When present together with the chaperonin, ATP--and to a lesser extent AMP-PNP--reduced the recovery yields and led to the resumption of aggregation. The use of the complete chaperonin system (GroEL, GroES, and ATP) eliminated the GroEL-mediated increase in recovery and folding proceeded less efficiently than in buffer alone. This unusual behavior can be explained in terms of a chaperonin "buffering" effect and the different affinities of GroE complexes for denatured beta-galactosidase. |
| Links |
PubMed PMC2143363 Online version:10.1002/pro.5560050309 |
| Keywords |
Adenosine Triphosphate/pharmacology; Adenylyl Imidodiphosphate/pharmacology; Bacterial Proteins/metabolism; Bacterial Proteins/pharmacology; Chaperonin 10/chemistry; Chaperonin 10/metabolism; Chaperonin 60/chemistry; Chaperonin 60/metabolism; Chaperonins; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli Proteins; Guanidine; Guanidines/pharmacology; Heat-Shock Proteins/metabolism; Heat-Shock Proteins/pharmacology; Models, Chemical; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Protein Conformation; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; beta-Galactosidase/chemistry; beta-Galactosidase/metabolism |
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