Protein folding in the cell: Competing models of chaperonin function

FASEB Journal

Volumn 10, Issue 1, 1996, Pages 20-26

  Ellis, R John ^b   Hartl, F Ulrich ^b  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b NONE

Author keywords

GroEL; GroES; molecular chaperones; protein folding

Indexed keywords

CHAPERONE; CHAPERONIN;

CONFORMATIONAL TRANSITION; ESCHERICHIA COLI; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REVIEW;

ESCHERICHIA COLI;

EID: 0030042460     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.1.8566542     Document Type: Review

References (43)

1. Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science (Wash.) 181, 223-230
2. Neidhardt, F. C. (1987) Chemical composition of Escherichia coli. In Escherichia coli and Salmonella typhimurium; cellular and molecular biology (Neidhardt, F. C., editor-in-chief) Vol. 2, pp. 1334-1345, American Society for Microbiology, Washington D.C.
3. Zimmerman, S. B., and Minton, A. P. (1993) Macromolecular crowding: biochemical, biophysical and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22, 27-65
4. Jaenicke, R. (1991) Protein folding: local structures, domains, subunits and assemblies. Biochemistry 30, 3147-3161
5. Ellis, R. J., and van der Vies, S. M. (1991) Molecular chaperones. Annu. Rev. Biochem. 60, 321-347
6. Ellis, R. J., Laskey, R. A., and Lorimer, G. H., eds (1993) Molecular Chaperones, 1st Ed, pp. 1-121, Chapman & Hall, London
7. Hendrick, J. P., and Hartl, F.-U. (1993) Molecular chaperone functions of heat shock proteins. Annu. Rev. Biochem. 62, 349-384
8. Hendrick, J. P., and Hartl, F.-U. (1995) The role of molecular chaperones in protein folding. FASEB. J. 9, 1559-1569
9. Hemmingsen, S. M., Woolford, C., van der Vies, S. M.,Tilly, K., Dennis, D. T., Georgopoulos, C. C., Hendrix, R. W., and Ellis, R. J. (1988) Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature (London) 333, 330-334
10. Kubota, H., Hynes, G., and Willison, K. (1995) The chaperonin containing t-complex polypeptide (TCP-1); multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur. J. Biochem. 230, 3-16
11. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., and Sigler, P. B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature (London) 371, 578-586
12. Ellis, R. J., ed (1996) The Chaperonins, Academic Press, Orlando, Florida In press
13. Goloubinoff, P., Christeller, J. P., Gatenby, A. A., and Lorimer, G. H. (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylasc from an unfolded state depends on two chaperonin proteins and ATP. Nature (London) 342, 884-889
14. Ellis, R. J. (1987) Proteins as molecular chaperones. Nature (London) 328, 378-379
15. Barraclough, R., and Ellis, R. J. (1980) Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact chloroplasts. Biochim. Biophys. Acta 608, 19-31
16. Martin, J., Langer, T., Boteva, R., Schramel, Horwich, A. L., and Hartl, F.-U. (1991) Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate. Nature (London) 352, 36-42
17. Robinson, C. V., Gross, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Haiti, F-U., Dobson, C. M., et al. (1994) Conformation of GroEL-bound alpha-lactalbumin probed by mass spectroscopy. Nature (London) 372, 646-651
18. Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F.-U. (1992) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765
19. Braig, K., Simon, M., Furuya, F., Hainfeld, J. F., and Horwich, A. L. (1993) A polypeptide bound by the chaperonin GroEL is located within a central cavity. Proc. Natl. Acad. Sci. USA 90, 3978-3982
20. Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R., and Saibil, H. R. (1994) Location of a folding protein and shape changes in GroEL-GroES imaged by cryo-electron microscopy. Nature (London) 371, 261-264
21. Fenton, W. A., Kashi, Y., Furtak, K., and Horwich, A. L. (1994) Residues in chaperonin GroEL required for polypeptide binding and release. Nature (London) 371, 614-619
22. Martin, J., Mayhew, M., Langer, T., and Haitl, F.-U. (1993) The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature (London) 366, 228-233
23. Saibil, H. R., Dong, Z., Wood, S., and auf der Mauer, A. (1991) Binding of chaperonins. Nature (London) 353, 25-26
24. Bochkareva, E. S., and Girshovich, A. S. (1994) ATP induces non-identity of two rings in GroEL. J. Biol. Chem. 269, 23869-23871
25. Hayer-Hartl, M. K., Martin, J., and Haiti, F.-U. (1995) Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science (Wash.) 269, 836-841
26. 7. FEBS Lett. 366, 17-20
27. Jackson, G. S., Staniforth, R. A., Halsall, D. J., Atkinson, T., Holbrook, J. J., Clarke, A. R., and Burston, S. G. (1993) Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Eur. J. Biochem. 32, 2554-2563
28. Todd, M. J., and Lorimer, G. H. (1995) Stability of the asymmetric Eschenchia coli chaperonin complex. J. Biol. Chem. 270, 5388-5394
29. Todd, M. J., Viitanen, P. V., and Lorimer, G. H. (1994) Dynamics of the chaperonin ATPase cycle; implications for facilitated protein folding. Science (Wash.) 265, 659-666
30. Schmidt, M., Rutkat, K., Rachel, R., Pfeifer, G., Jaenicke, R., Viitanen, P., Lorimer, G., and Buchner, J. (1994) Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (Wash.) 265, 656-659
31. Engel, A., Hayer-Hartl, M. K., Goldie, K. N., Pfeifer, G., Hegerl, R., Muller, S., da Silva, A. C. R., Baumeister, W., and Hartl, F.-U. (1995) Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science (Wash.) 269, 832-836
32. Burston, S. G., Ranson, N. A., and Claike, A. R. (1995) The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138-152
33. 2 chaperonin hetero-oligomer. Science (Wash.) 265, 653-656
34. Ellis, R. J. (1994) Opening and closing the Anfinsen cage. Curr. Biol. 4, 633-635
35. Gray, T. E., and Fersht, A. R. (1991) Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 292, 254-258
36. Schmidt, M., Buchner, J., Todd, M. J., Lorimer, G. H., and Viitanen, P. V. (1994) On the role of GroES in the chaperonin-assisted folding reactions: three case studies. J. Biol. Chem. 269, 10304-10311
37. Ostermann, J., Horwich, A. L., Neupert, W.,and Hartl, F.-U. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature (London) 341, 125-130
38. Weissman, J. S., Kashi, Y., Fenton, W. A., and Horwich, A. L. (1994) GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78, 693-702
39. Bochkareva, E. S., and Girshovich, A. S. (1994) A newly synthesised protein interacts with GroES on the surface of chaperonin GroEL. J. Biol. Chem. 267, 25672-25675
40. Ranson, N. A., Dunster, N. J., Burston, S. G., and Clarke, A. R. (1995) Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250, 581-586
41. Peralta, D., Hartman, D. J., Hoogenraad, N. J., and Hoj, P. B. (1994) Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Lett. 339, 45-49
42. Gray, T. E., and Fersht, A. R. (1993) Refolding of barnase in the presence of GroE. J. Mol. Biol. 232, 1197-1207
43. Horwich, A. L., Low, K. B., Fenton, F. A., Hirshfield, I. N., and Furtak, K. (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GioEL. Cell 74, 909-917