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Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding

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Abstract

GroEL is thought to assist protein folding in part by providing a passive 'box' in which folding can occur without danger of aggregation. Two new papers now suggest that GroEL can also play a more active role by promoting rearrangement and even unfolding of kinetic folding intermediates.

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Figure 1: Schematic of the GroEL reaction cycle.
Figure 2: Hypothetical 'kinetic-editing' model for selection of GroEL substrates.
Figure 3: A model for GroES and ATP-dependent unfolding.

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Acknowledgements

We thank G. Lorimer and P. Sigler for Fig. 3, and members of the Weissman lab for helpful comments.

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Authors and Affiliations

  1. the Department of Cellular & Molecular Pharmacology, University of California- San Francisco, 513 Parnassus Ave, San Francisco, 94143-0450, California, USA

    Jue D. Wang & Jonathan S. Weissman

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  1. Jue D. Wang
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  2. Jonathan S. Weissman
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Correspondence to Jonathan S. Weissman.

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Wang, J., Weissman, J. Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding. Nat Struct Mol Biol 6, 597–600 (1999). https://doi.org/10.1038/10636

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