NDLI: Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.

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Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Baneyx, F. Ayling, A.
Description	Country affiliation: United States Author Affiliation: Ayling A ( Department of Chemical Engineering, University of Washington, Seattle 98195-1750, USA.)
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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Pharmacology Escherichia Coli Enzymology Heat-shock Proteins Protein Folding Beta-galactosidase Chemistry Metabolism Adenosine Triphosphate Adenylyl Imidodiphosphate Chaperonin 10 Chaperonin 60 Chaperonins Electrophoresis, Polyacrylamide Gel Escherichia Coli Proteins Guanidine Guanidines Models, Chemical Molecular Chaperones Protein Conformation Protein Denaturation Spectrometry, Fluorescence Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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