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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

Nature volume 366, pages 228–233 (1993)Cite this article

Abstract

The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.

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Author notes

  1. Thomas Langer

    Present address: Institut für Physiologische Chemie, Goethestrasse 33, 80336, Munchen, Germany

Authors and Affiliations

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

    Jörg Martin, Mark Mayhew, Thomas Langer & Ulrich Hartl

Authors
  1. Jörg Martin
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  2. Mark Mayhew
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  3. Thomas Langer
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  4. Ulrich Hartl
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Martin, J., Mayhew, M., Langer, T. et al. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366, 228–233 (1993). https://doi.org/10.1038/366228a0

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