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Protein folding in the central cavity of the GroEL–GroES chaperonin complex

Nature volume 379, pages 420–426 (1996)Cite this article

Abstract

The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage. Folded dihydrofolate reductase emerges upon ATP-dependent GroES release. Other proteins, such as rhodanese, may leave GroEL after having attained a conformation that is committed to fold. Incompletely folded polypeptide rebinds to GroEL, resulting in structural rearrangement for another folding trial in the chaperonin cavity.

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Author notes

  1. Jörg Martin

    Present address: Department of Molecular and Cell Biology and Biochemistry, Brown University, Box G-J2, Providence, Rhode Island, 02912, USA

Authors and Affiliations

  1. Cellular Biochemistry and Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York, 10021, USA

    Mark Mayhew, Ana C. R. da Silva, Jörg Martin & F. Ulrich Hartl

  2. Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York, 10021, USA

    Hediye Erdjument-Bromage & Paul Tempst

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  6. F. Ulrich Hartl
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Mayhew, M., da Silva, A., Martin, J. et al. Protein folding in the central cavity of the GroEL–GroES chaperonin complex. Nature 379, 420–426 (1996). https://doi.org/10.1038/379420a0

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