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Protein folding Folding with a two-stroke motor

Nature volume 388, pages 720–721 (1997)Cite this article

One of the hot problems in modern biology is how the molecular chaperone GroEL, along with its cohort GroES, facilitates the folding of other proteins. It is a wonderfully complex and highly dynamic process, the details of which are only beginning to emerge. Two papers by Xu et al.1 and Rye et al.2 from Yale University (pages and of this issue) mark considerable progress in our understanding, and again demonstrate the power of crystallography1 coupled to clever mutagenesis2. They also remind us that we still have lots to do before the mechanism of this remarkable two-stroke folding machine can be considered to be ‘defined’.

The interaction between GroEL and GroES is necessary for certain proteins to fold under otherwise non-permissive conditions3. The subunits of both proteins are heterologously assembled into heptameric rings4,5. In the case of GroEL, two rings stack back-to-back (isologously) to form the native 14-mer, enclosing two large, non-contiguous central cavities. Each monomer unit consists of three domains. The larger ‘equatorial’ and ‘apical’ domains are linked through a smaller ‘intermediate’ domain.

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Figure 1: The crystal structure of the asymmetrical GroES7-GroEL14 complex, solved by Xu et al.1, provides new insights into how GroEL and GroES mediate the folding of other proteins.
Figure 2: Rye et al.2 have used mutagenesis to explore the mechanism of protein folding by GroES/GroEL.
Figure 3: Rye et al. have used mutagenesis to explore the mechanism of protein folding by GroES/GroEL.

References

  1. Xu, Z., Horwich, A. L. & Sigler, P. B. Nature 388, 741–749 (1997).

    Article  ADS  CAS  Google Scholar 

  2. Rye, H. S. et al. Nature 388, 792–798 (1997).

    Google Scholar 

  3. Schmidt, M., Buchner, J., Todd, M. J., Lorimer, G. H. & Viitanen, P. V. J. Biol. Chem. 269, 10304–10311 (1994).

    Google Scholar 

  4. Braig, K. et al. Nature 271, 578–586 (1994).

    Google Scholar 

  5. Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L. & Deisenhofer, J. Nature 379, 37–45 (1996).

    Article  ADS  CAS  Google Scholar 

  6. Landry, S. J., Zeilstra-Ryalls, J., Fayet, O., Georgopoulos, C. & Gierasch, L. M. Nature 364, 255–258 (1993).

    Article  ADS  CAS  Google Scholar 

  7. Chandrasekhar, G. N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. J. Biol. Chem. 261, 12414–12419 (1986).

    Google Scholar 

  8. Langer, T., Pfeifer, G., Martin, J., Baumeister, W. & Hartl, F. U. EMBO J. 11, 4757–4765 (1992).

    Google Scholar 

  9. Azem, A., Kessel, M. & Goloubinoff, P. Science 265, 653–656 (1994).

    Google Scholar 

  10. Schmidt, M. et al. Science 265, 656–659 (1994).

    Google Scholar 

  11. Roseman, A. M., Chen, S., White, H., Braig, K. & Saibil, H. R. Cell 87, 241–251 (1996).

    Google Scholar 

  12. Weissman, J. S. et al. Cell 83, 577–587 (1995).

    Google Scholar 

  13. Sparrer, H., Rutkat, K. & Buchner, J. Proc. Natl Acad. Sci. USA 94, 1096–1100 (1997).

    Google Scholar 

  14. Todd, M. J., Viitanen, P. V. & Lorimer, G. H. Science 265, 659–666 (1994).

    Google Scholar 

  15. Weismann, J. S., Kashi, Y., Fenton, W. A. & Horwich, A. L. Cell 78, 693–702 (1994).

    Google Scholar 

  16. Ranson, N. A., Burston, S. G. & Clarke, A. R. J. Mol. Biol. 266, 656–664 (1997).

    Google Scholar 

  17. Viitanen, P. V., Gatenby, A. A. & Lorimer, G. H. Protein Sci. 1, 361–369 (1992).

    Google Scholar 

  18. Lin, S., Schwarz, F. P. & Eisenstein, E. J. Biol. Chem. 270, 14581–14587 (1995).

    Google Scholar 

  19. Fenton, W. A., Kashi, Y., Furtak, K. & Horwich, A. L. Nature 371, 578–586 (1994).

    Article  Google Scholar 

  20. Buckle, A. M., Zahn, R. & Fersht, A. R. Proc. Natl Acad. Sci. USA 94, 3571–3575 (1997).

    Google Scholar 

  21. Jackson, G. S. et al. Biochemistry 32, 2554–2563 (1993).

    Google Scholar 

  22. Todd, M. J., Lorimer, G. H. & Thirumalai, D. Proc. Natl Acad. Sci. USA 93, 4030–4034 (1996).

    Google Scholar 

  23. Zahn, R., Perrett, S., Stenberg, G. & Fersht, A. R. Science 271, 642–645 (1996).

    Google Scholar 

  24. Boisvert, D. C., Wang, J., Otwinowski, Z., Horwich, A. L. & Sigler, P. B. Nature Struct. Biol. 3, 170–177 (1996).

    Google Scholar 

  25. Murai, N., Makino, Y. & Yoshida, M. J. Biol. Chem. 271, 28229–28234 (1996).

    Google Scholar 

  26. Azem, A., Diamant, S., Kessel, M., Weiss, C. & Goloubinoff, P. Proc. Natl Acad. Sci. USA 92, 12021–12025 (1995).

    Google Scholar 

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  1. Du Pont Company is currently at Biochemie II, Universitätstrasse 31, D-93040, Regensburg, Germany

    George Lorimer

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Lorimer, G. Protein folding Folding with a two-stroke motor. Nature 388, 720–721 (1997). https://doi.org/10.1038/41892

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