Summary
Chaperonin-facilitated folding of proteins involves two partial reactions. The first partial reaction, the formation of stable binary complexes between chaperonin-60 and non-native states of the target protein, is common to the chaperonin-facilitated folding of all target proteins investigated to date. The structural basis for this interaction is not presently understood. The second partial reaction, the dissociation of the target protein in a form committed to the native state, appears to proceed by a variety of mechanisms, dependent upon the nature of the target protein in question. Those target proteins (e.g. rubisco, rhodanese, citrate synthase) which require the presence of chaperonin-10, also appear to require the hydrolysis of ATP to bring about the dissociation of the target protein from chaperonin-60. With one exception (pre-β-lactamase) those target proteins which do not require the presence of chaperonin-10 to be released from chaperonin-60, also do not require the hydrolysis of ATP, since non-hydrolysable analogues of ATP support the release of the target protein in a state committed to the native state. The question of whether or not chaperonin-facilitated folding constitutes a catalysed event is addressed.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Anfinsen, C.B. 1973 Principles that govern the folding of protein chains. Science, Wash. 181, 223–230.
Badcoe, I.G., Smith, C.J., Wood, S. et al. 1991 Binding of a chaperonin to the folding intermediate of lactate dehydrogenase. Biochemistry 30, 9195–9200.
Barraclough, R. & Ellis, R.J. 1980 Protein synthesis in chloroplasts. IX. Assembly of newly synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochem. biophys. Acta 608, 19–31.
Buchner, J., Schmidt, M., Fuchs, M. et al. 1990 GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586–1591.
Creighton, T.E. 1985 Folding of proteins adsorbed reversibly to ion-exchange resins. In Protein structure, folding and design (ed. D. L. Oxender), pp. 249–257. New York: Alan R. Liss.
Fisher, M.T. 1992 Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP. Biochemistry 31, 3955–3963.
Goldberg, M., Rudolph, R. & Jaenicke, R. 1991 A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30, 2791–2797.
Goloubinoff, P., Gatenby, A.A. & Lorimer, G.H. 1989a GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature, Lond. 337, 44–47.
Goloubinoff, P., Christeller, J.T., Gatenby, A.A. & Lorimer, G.H. 1989b Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP. Nature, Lond. 342, 884–889.
Hemmingsen, S.M., Woolford, C., van der Vies, S.M. et al. 1988 Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature, Lond. 333, 330–334.
Hendrix, R.W. 1979 Purification and properties of groE, a host protein involved in bacteriophage lambda assembly. J. molec. Biol. 129, 375–392.
Höll-Neugebauer, B., Rudolph, R., Schmidt, M. & Buchner, J. 1991 Reconstitution of a heat shock effect in vitro: Influence of GroE on the thermal aggregation of α-glucosidase from yeast. Biochemistry 30, 11609–11614.
Laminet, A.A., Ziegelhoffer, T., Georgopoulos, C. & Plückthum, A. 1990 The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J. 9, 2315–2319.
Landry, S.J. & Gierasch, L.M. 1991 The chaperonin GroEL binds a polypeptide in an α-helical conformation. Biochemistry 30, 7359–7362.
Langer, T., Lu, C., Echols, H., Flanagan, J. et al. 1992 Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature, Lond. 356, 683–689.
Lee, S.C. & Olins, P.O. 1992 Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli. J. biol. Chem. 267, 2849–2852.
Lolis, E. & Petsko, G.A. 1990 Transition-state analogues in protein crystallography: Probes of the structural source of enzyme catalysis. A. Rev. Biochem. 59, 597–630.
Martin, J., Langer, T., Boteva, R. et al. 1991 Chaperonin-mediated protein folding at the surface of groEL through a ‘molten globule’-like intermediate. Nature, Lond. 352, 36–42.
Mendoza, J., Rogers, E., Lorimer, G.H. & Horowitz, P. 1991 Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. biol. Chem. 266, 13044–13049.
Mendoza, J., Lorimer, G.H. & Horowitz, P. 1992 Chaperonin cpn60 from E. coli protects rhodanese against heat inactivation and supports folding at elevated temperatures. J. biol. Chem. 267, 17631–17634.
Mitraki, A. & King, J. 1989 Protein folding intermediates and inclusion body formation. Bio Technology 7, 690–697.
Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N. & Kawata, Y. 1992 Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP. J. biol. Chem. 267, 17773–17779.
Pauling, L. 1946 Molecular architecture and biological reactions. Chem. Engng News 24, 1375–1377.
Roy, H., Bloom, M., Milos, P. & Monroe, M. 1982 Studies on the assembly of ribulose bisphosphate carboxylase in isolated pea chloroplasts. J. Cell Biol. 94, 20–27.
Schmidt, M. & Buchner, J. 1992 Interaction of GroEL with an all-b-protein J. biol. Chem. 267, 16829–16833.
Teuten, A.J., Smith, R.A.G. & Dobson, C.M. 1991 Domain interactions in human plasminogen studied by 1H NMR. FEBS Lett. 278, 17–22.
Tilly, K. & Georgopoulos, C. 1982 Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo. J. Bact. 149, 1082–1088.
van der Vies, S.M., Viitanen, P.V., Gatenby, A.A., Lorimer, G.H. & Jaenicke, R. 1992 Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. Biochemistry 31, 3635–3644.
Viitanen, P.V., Lubben, T.H., Reed, J. et al. 1990 Chaperonin facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. Biochemistry 26, 5665–5671.
Viitanen, P.V., Donaldson, G.K., Lorimer, G.H., Lubben, T.H. & Gatenby, A.A. 1991 Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry 30, 9716–9723.
Viitanen, P.V., Gatenby, A.A. & Lorimer, G.H. 1992a Purified chaperonin 60 (GroEL) interacts with the non-native states of a multitude of Escherichia coli proteins. Protein Sci. 1, 363–369.
Viitanen, P.V., Lorimer, G.H., Seetharam, R. et al. 1992b Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. J. biol. Chem. 267, 695–698.
Wynn, R.M., Davie, J.R., Cox, R.P. & Chuang, D.T. 1992 Chaperonins GroEL and GroES promote assembly of heterotetramers (α2β2) of mammalian mitochondrial branched chain α-keto acid decarboxylase in Escherichia coli. J. biol. Chem. 267, 12400–12403.
Zhi, W., Landry, S., Gierasch, L.M. & Srere, P.A. 1992 Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci. 1, 522–529.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Lorimer, G.H., Todd, M.J., Viitanen, P.V. (1993). Chaperonins and protein folding: unity and disunity of mechanisms. In: Ellis, R.J., Laskey, R.A., Lorimer, G.H. (eds) Molecular Chaperones. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2108-8_6
Download citation
DOI: https://doi.org/10.1007/978-94-011-2108-8_6
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-4935-1
Online ISBN: 978-94-011-2108-8
eBook Packages: Springer Book Archive