Abstract
THE important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 (ref. 1) is a typical molecular chaperone2,3. It possesses ATPase activity4,5 and interacts in ATP-driven reactions with non-folded proteins6–8 to stimulate their correct folding and/or assembly by preventing the formation of improper protein structures or aggregates7,9–11. As GroEL is isolated and functions as a 20–25S tetradecameric particle5,6,12 (GroELp), the question arises—what is the mechanism of its own assembly? Here we show the (Mg–ATP)-dependent self-stimulation ('self-chaperoning') in vitro of GroELp reassembly from its monomeric state.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Hemmingsen, S. M. et al. Nature 333, 330–334 (1988).
Ellis, R. J. Nature 328, 378–379 (1987).
Ellis, R. J. & Hemmingsen, S. M. Trends biochem. Sci. 14, 339–342 (1989).
Ishihama, A., Ukeichi, T., Matsumoto, A. & Yamamoto, S. J. Biochem., Tokyo 79, 927–936 (1976).
Hendrix, R. W. J. molec. Biol. 129, 375–392 (1979).
Bochkareva, E. S., Lissin, N. M. & Girshovich, A. S. Nature 336, 254–257 (1988).
Goloubinoff, P., Christeller, J. T., Gatenby, A. A. & Lorimer, G. H. Nature 432, 884–889 (1989).
Lecker, S. et al. EMBO J. 8, 2703–2709 (1989).
Friedman, D. I., Olson, E. R., Georgopoulos, C., Tilly, K., Hershowitz, I. & Banuett, F. Microbiol. Rev. 48, 299–325 (1984).
Goloubinoff, P., Gatenby, A. A. & Lorimer, G. H. Nature 337, 44–47 (1989).
Van Dyk, T. K., Gatenby, A. A. & LaRossa, R. A. Nature 342, 451–453 (1989).
Hohn, T., Hohn, B., Engel, A., Wurtz, M. & Smith, P. R. J. molec. Biol. 129, 359–373 (1979).
Priyalov, P. L. Rev. Biophys. biophys. Chem. 18, 47–69 (1989).
Privalov, P. L. & Gill, S. J. Adv. Prot. Chem. 39, 191–324 (1988).
Pelham, H. R. B. Cell 46, 959–961 (1986).
Rothman, J. E. Cell 59, 591–601 (1989).
Kassenbrock, C. K. & Kelly, R. B. EMBO J. 8, 1461–1467 (1989).
Laminet, A. A., Ziegelhoffer, T., Georgopoulos, C. & Pluckthun, A. EMBO J. 9, 2315–2319 (1990).
Chandrasekhar, G. N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. J. biol. Chem. 261, 12414–12419 (1986).
McLellan, T. Analyt. Biochem. 126, 94–99 (1982).
Provencher, S. W. & Glockner, J. Biochemistry 20, 33–37 (1981).
Jaenicke, L. Analyt. Biochem. 61, 623–627 (1974).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Lissin, N., Venyaminov, S. & Girshovich, A. (Mg–ATP)-dependent self-assembly of molecular chaperone GroEL. Nature 348, 339–342 (1990). https://doi.org/10.1038/348339a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/348339a0
This article is cited by
-
Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL
Journal of Chemical Biology (2014)
-
Physiological responses of Escherichia coli exposed to different heat-stress kinetics
Archives of Microbiology (2010)
-
Phosphofructokinase interacts with molecular chaperonins GroEL and GroES
Acta Biologica Hungarica (1997)
-
Protein folding in the central cavity of the GroEL–GroES chaperonin complex
Nature (1996)
-
Molecular chaperones and protein folding in plants
Plant Molecular Biology (1996)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
