Skip to main content
SpringerLink
Log in

Characterization of a functionally important mobile domain of GroES

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

ALTHOUGH genetic1 and biochemical2,3 evidence has established that GroES is required for the full function of the molecular chaperone, GroEL, little is known about the molecular details of their interaction. GroES enhances the cooperativity of ATP binding and hydrolysis by GroEL (refs 4, 5) and is necessary for release and folding of several GroEL substrates6. Here we report that native GroES has a highly mobile and accessible polypeptide loop whose mobility and accessibility are lost upon formation of the GroES/GroEL complex. In addition, lesions present in eight independently isolated mutant groES alleles map in the mobile loop. Studies with synthetic peptides suggest that the loop binds in a hairpin conformation at a site on GroEL that is distinct from the substrate-binding site. Flexibility may be required in the mobile loops on the GroES seven-mer to allow them to bind simultaneously to sites on seven GroEL subunits, which may themselves be able to adopt different arrangements, and thus to modulate allosterically GroEL/substrate affinity.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Tilly, K. & Georgopoulos, C. J. Bact. 149, 1082–1088 (1982).

    CAS  PubMed  Google Scholar 

  2. Chandrasekhar, G. N. et al. J. biol. Chem. 261, 12414–12419 (1986).

    CAS  PubMed  Google Scholar 

  3. Goloubinoff, P. et al. Nature 342, 884–889 (1989).

    Article  ADS  CAS  Google Scholar 

  4. Gray, T. E. & Fersht, A. R. FEBS Lett. 292, 254–258 (1991).

    Article  CAS  Google Scholar 

  5. Bochkareva, E. S. et al. J. biol. Chem. 267, 6796–6800 (1992).

    CAS  PubMed  Google Scholar 

  6. Jaenicke, R. Curr. Opin. struct. Biol. 3, 104–112 (1993).

    Article  CAS  Google Scholar 

  7. Wuthrich, K. NMR of Proteins and Nucleic Acids (Wiley, New York, 1986).

    Book  Google Scholar 

  8. Wishart, D. S., Sykes, B. D. & Richards, F. M. J. molec. Biol. 222, 311–333 (1991).

    Article  CAS  Google Scholar 

  9. Georgopoulos, C. P. et al. J. molec. Biol. 76, 45–60 (1973).

    Article  CAS  Google Scholar 

  10. Landry, S. J. & Gierasch, L. M. Biochemistry 30, 7359–7362 (1991).

    Article  CAS  Google Scholar 

  11. Landry, S. J. et al. Nature 355, 455–457 (1992).

    Article  ADS  CAS  Google Scholar 

  12. Langer, T. et al. EMBO J. 11, 4757–4765 (1992).

    Article  CAS  Google Scholar 

  13. Hartman, D. J. et al. Proc. natn. Acad. Sci. U.S.A. 89, 3394–3398 (1992).

    Article  ADS  CAS  Google Scholar 

  14. Lubben, T. H. et al. Proc. natn. Acad. Sci. U.S.A. 87, 7683–7687 (1990).

    Article  ADS  CAS  Google Scholar 

  15. Bertsch, U. et al. Proc. natn. Acad. Sci. U.S.A. 89, 8696–8700 (1992).

    Article  ADS  CAS  Google Scholar 

  16. Ohtaka, C., Nakamura, H. & Ishikawa, H. J. Bact. 174, 1869–1874 (1992).

    Article  CAS  Google Scholar 

  17. Martin, J. et al. Nature 352, 36–42 (1991).

    Article  ADS  CAS  Google Scholar 

  18. Creighton, T. E. Nature 352, 17–18 (1991).

    Article  ADS  CAS  Google Scholar 

  19. Mendoza, J. A. et al. J. biol. Chem. 266, 13044–13049 (1991).

    CAS  PubMed  Google Scholar 

  20. Nilsson, B & Anderson, S. A. Rev. Microbiol. 45, 607–635 (1991).

    Article  CAS  Google Scholar 

  21. Hemmingsen, S. M. et al. Nature 333, 330–334 (1988).

    Article  ADS  CAS  Google Scholar 

  22. Schagger, H. & von Jagow, G. Analyt. Biochem. 166, 368–379 (1987).

    Article  CAS  Google Scholar 

  23. Marion, D., Ikura, M. & Bax, A. J. magn. Reson. 84, 425–430 (1989).

    ADS  CAS  Google Scholar 

  24. Braig, K. et al. Proc. natn. Acad. Sci. U.S.A. 90, 3978–3982 (1993).

    Article  ADS  CAS  Google Scholar 

Download references

Author information

Author notes

  1. Samuel J. Landry

    Present address: Department of Biochemistry SL43, Tulane University School of Medicine, 1430 Tuiane Avenue, New Orleans, Louisiana, 70112, USA

  2. Jill Zeilstra-Ryalls

    Present address: Department of Microbiology, University of Texas Medical School, 6431 Fannin, Houston, Texas, 77225, USA

  3. Olivier Fayet

    Present address: Microbiology and Molecular Genetics-CNRS, 118 route de Narbonne, 31062, Toulouse, France

Authors and Affiliations

  1. University of Texas Southwestern Medical Center, Dallas, Texas, 75235-9041, USA

    Samuel J. Landry & Lila M. Gierasch

  2. Département de Biochimie Médicale, Universite de Genève, 1211, Genève, 4, Switzerland

    Jill Zeilstra-Ryalls, Olivier Fayet & Costa Georgopoulos

  3. University of Utah Medical Center, Salt Lake City, Utah, 84132, USA

    Costa Georgopoulos

Authors
  1. Samuel J. Landry
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jill Zeilstra-Ryalls
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Olivier Fayet
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Costa Georgopoulos
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Lila M. Gierasch
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Landry, S., Zeilstra-Ryalls, J., Fayet, O. et al. Characterization of a functionally important mobile domain of GroES. Nature 364, 255–258 (1993). https://doi.org/10.1038/364255a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/364255a0

  • Springer Nature Limited

This article is cited by

Search

Navigation