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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

Nature volume 352, pages 36–42 (1991)Cite this article

Abstract

Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg–ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.

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Author notes

  1. Raina Boteva and Andrea Schramel: Zoologisches Institut der Universität München, Luisenstrasse 14, W-8000 München 2, Germany

  2. Arthur L. Horwich: Howard Hughes Medical Institute and Department of Human Genetics, Yale School of Medicine, 333 Cedar Street, New Haven, Connecticut 06510, USA

  3. F.-Ulrich Hartl: To whom correspondence should be addressed. Address after November 1: Laboratory of Cellular Biochemistry, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021, USA.

Authors and Affiliations

  1. Institut für Physiologische Chemie der Universität München, Goethestrasse 33, W-8000, München, 2, Germany

    Jörg Martin, Thomas Langer, Raina Boteva, Andrea Schramel, Arthur L. Horwich & F.-Ulrich Hartl

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Martin, J., Langer, T., Boteva, R. et al. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36–42 (1991). https://doi.org/10.1038/352036a0

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