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
Hauptverfasser: Grallert, Holger, Rutkat, Kerstin, Buchner, Johannes
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container_title The Journal of biological chemistry
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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.
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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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