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

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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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