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Group II chaperonin in an open conformation examined by electron tomography

Nature Structural Biology volume 5, pages 855–857 (1998)Cite this article

Thermosomes are archaeal members of the group II (or TCP-1 subclass) chaperonins which, together with the group I (or GroEL subclass) chaperonins, represent a distinct family of ubiquitous sequence-related molecular chaperones whose function is to assist in vivo protein folding. All chaperonins are large homo- or hetero-oligomeric complexes possessing ATPase activity. The subunits are arranged in two rings stacked together back-to-back, thus forming toroidal structures that provide an internal cavity for sequestering protein folding from the crowded environment of the cell (for a recent review see ref. 1). Group I chaperonins contain seven subunits in each ring, whereas group II chaperonins contain eight to nine2,3. Thermosomes from Thermoplasma acidophilum are hexadecamers composed of two subunits, α and β, which are 63% identical4, and alternate within the rings5. A central mass is visible on electron micrographs of ice-embedded thermosomes which probably corresponds to residual bound substrate. Both subunits can be expressed separately in Escherichia coli and are able to form homo-oligomeric complexes (α-only and β-only thermosomes), albeit with different stabilities6. Both, α+β and α-only thermosomes bind denatured substrates. However, in vitro refolding assays remain inconclusive so far, possibly because the refolding reaction requires the presence of prefoldin-like cofactors7; indeed, homologs of prefoldin exist in archaea.

Cryo-electron tomography of thermosomes

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Figure 1: Averaged side views of a, α-only and b, α+β thermosomes, embedded in vitreous ice.
Figure 2: a — Transparent tomographic three-dimensional map of the α-only thermosome in side view orientation with composite model placed into it.

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Acknowledgements

We would like to thank R. Hegerl for advice and many helpful discussions. This work was supported by the Deutsche Forschungsgemeinschaft (Priority Program: New Microscopical Techniques in Biology and Medicine).

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Authors and Affiliations

  1. Department of Structural Biology, Max Planck Institute for Biochemistry, D-82152, Martinsried, Germany

    Michael Nitsch, Jochen Walz, Dieter Typke, Martin Klumpp & Wolfgang Baumeister

  2. Department of Membrane Biochemistry, Max Planck Institute for Biochemistry, D-82152, Martinsried, Germany

    Lars-Oliver Essen

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Correspondence to Wolfgang Baumeister.

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Nitsch, M., Walz, J., Typke, D. et al. Group II chaperonin in an open conformation examined by electron tomography . Nat Struct Mol Biol 5, 855–857 (1998). https://doi.org/10.1038/2296

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