Limits of Protein Folding Inside GroE Complexes
The GroE chaperones of Escherichia coli promote the folding of other proteins under conditions where no spontaneous folding occurs. One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermole...
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Veröffentlicht in: | The Journal of biological chemistry 2000-07, Vol.275 (27), p.20424-20430 |
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creator | Grallert, Holger Rutkat, Kerstin Buchner, Johannes |
description | The GroE chaperones of Escherichia coli promote the folding of other proteins under conditions where no spontaneous folding occurs. One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermolecular interactions during folding. We show here that, especially for oligomeric proteins, the timing of encapsulation and release is of critical importance. If this cycle is decelerated, misfolding is observed inside functional chaperone complexes. |
doi_str_mv | 10.1074/jbc.M002243200 |
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One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermolecular interactions during folding. We show here that, especially for oligomeric proteins, the timing of encapsulation and release is of critical importance. 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subjects | Adenosine Triphosphatases - metabolism Bacterial Proteins - chemistry Bacterial Proteins - ultrastructure Chaperonin 10 - chemistry Chaperonin 60 - chemistry Chaperonins Citrate (si)-Synthase - chemistry Dimerization Escherichia coli Escherichia coli Proteins Heat-Shock Proteins - chemistry Heat-Shock Proteins - ultrastructure Kinetics Microscopy, Electron Molecular Chaperones - chemistry Protein Folding Temperature Time Factors |
title | Limits of Protein Folding Inside GroE Complexes |
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