Reconciling theories of chaperonin accelerated folding with experimental evidence |
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Authors: | Andrew I Jewett Joan-Emma Shea |
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Institution: | (1) Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA;(2) Department of Physics, University of California, Santa Barbara, CA 93106, USA; |
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Abstract: | For the last 20 years, a large volume of experimental and theoretical work has been undertaken to understand how chaperones
like GroEL can assist protein folding in the cell. The most accepted explanation appears to be the simplest: GroEL, like most
other chaperones, helps proteins fold by preventing aggregation. However, evidence suggests that, under some conditions, GroEL
can play a more active role by accelerating protein folding. A large number of models have been proposed to explain how this
could occur. Focused experiments have been designed and carried out using different protein substrates with conclusions that
support many different mechanisms. In the current article, we attempt to see the forest through the trees. We review all suggested
mechanisms for chaperonin-mediated folding and weigh the plausibility of each in light of what we now know about the most
stringent, essential, GroEL-dependent protein substrates. |
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