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The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

Nature Structural Biology volume 1, pages 439–446 (1994)Cite this article

Abstract

We investigate here the interaction between GroEL and two kinds of non-native α-lactalbumin. α-Lactalbumin is a Ca2+-binding protein which assumes a molten globule state in the absence of Ca2+ (apo-α-lactalbumin) at neutral pH. Our results, obtained by molecular-sieve chromatography and hydrogen-exchange measurements, show that apo-α-lactalbumin in this molten globule state is not bound to GroEL either in the absence or in the presence of KCl. On the other hand, we show by molecular-sieve chromatography that α-lactalbumin, in which the four disulphide bonds are fully reduced, is bound to GroEL when 50 mM KCl is present. The results demonstrate that the protein state recognized by GroEL is more unfolded and expanded than the typical molten globule state of α-lactalbumin.

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Authors and Affiliations

  1. Department of Physics, School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113, Japan

    Akira Okazaki, Teikichi Ikura, Kiyokazu Nikaido & Kunihiro Kuwajima

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  1. Akira Okazaki
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  2. Teikichi Ikura
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  3. Kiyokazu Nikaido
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  4. Kunihiro Kuwajima
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Okazaki, A., Ikura, T., Nikaido, K. et al. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nat Struct Mol Biol 1, 439–446 (1994). https://doi.org/10.1038/nsb0794-439

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