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A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A

Nature volume 354, pages 408–410 (1991)Cite this article

Abstract

THE 'molten' globular conformation of a protein is compact with a native secondary structure but a poorly defined tertiary structure1,2. Molten globular states are intermediates in protein folding and unfolding3–5 and they may be involved in the translocation or insertion of proteins into membranes6. Here we investigate the membrane insertion of the pore-forming domain of colicin A, a bacteriocin that depolarizes the cytoplasmic membrane of sensitive cells7–9. We find that this poreforming domain, the insertion of which depends on pH (refs 10,11), undergoes a native to molten globule transition at acidic pH. The variation of the kinetic constant of membrane insertion of the protein into negatively charged lipid vesicles as a function of the interfacial pH correlates with the appearance of the acidic molten globular state, indicating that this state could be an intermediate formed during the insertion of colicin A into membranes.

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Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, D-6900, Heidelberg, Germany

    F. G. van der Goot, J. M. González-Mañas, J. H. Lakey & F. Pattus

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  1. F. G. van der Goot
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  2. J. M. González-Mañas
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  3. J. H. Lakey
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  4. F. Pattus
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van der Goot, F., González-Mañas, J., Lakey, J. et al. A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354, 408–410 (1991). https://doi.org/10.1038/354408a0

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