Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL

Journal of Molecular Biology

Volumn 264, Issue 4, 1996, Pages 643-649

  Katsumata, Kumiko ^a   Okazaki, Akira ^a   Tsurupa, Galina P ^a   Kuwajima, Kunihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Chaperonin; Groel; Molten globule state; Protein folding; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CATION; CHAPERONIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENTROPY; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; IONIC STRENGTH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; TEMPERATURE SENSITIVITY; THERMODYNAMICS;

EID: 0030582682     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0666     Document Type: Editorial

References (44)

1. Arai, M. & Kuwajima, K. (1996). Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Des. 1, 275-287.
2. Baldwin, R. L. (1986). Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl Acad. Sci. USA, 83, 8069-8072.
3. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L. & Sigler, P. B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature, 371, 578-586.
4. Braig, K., Adams, P. D. & Brünger, A. T. (1995). Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2, 1083-1094.
5. Brissette, P., Ballou, D. P. & Massey, V. (1989). Determination of the dead time of a stopped-flow fluorometer. Anal. Biochem. 181, 234-238.
6. Buchner, J. (1996). Supervising the fold: Functional principles of molecular chaperones. FASEB J. 10, 10-19.
7. Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R. & Salbil, H. R. (1994). Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature, 371, 261-264.
8. Corrales, F. J. & Fersht, A. R. (1995). The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding. Proc. Natl Acad. Sci. USA, 92, 5326-5330.
9. Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
10. Ellis, R. J. & Hartl, F. U. (1996). Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10, 20-26.
11. Fenton, W. A., Kashi, Y., Furtak, K. & Horwich, A. L. (1994). Residues in chaperonin GroEL required for polypeptide binding and release. Nature, 371, 614-619.
12. Gibbons, D. L. & Horowitz, P. M. (1995). Exposure hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401. J. Biol. Chem. 270, 7335-7340.
13. Gray, T. E., Eder, J., Bycroft, M., Day, A. G. & Fersht, A. R. (1993). Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL. EMBO J. 12, 4145-4150.
14. Hartl, F. U. & Martin, J. (1995). Molecular chaperones in cellular protein folding. Curr. Opin. Struct. Biol. 5, 92-102.
15. Hayer-Hartl, M. K., Ewbank, J. J., Creighton, T. E. & Hartl, F. U. (1994). Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin. EMBO J. 13, 3192-3202.
16. Hiraoka, Y. & Sugai, S. (1984). Thermodynamics of thermal unfolding of bovine apo-α-lactalbumin. Int. J. Pept. Protein Res. 23, 535-542.
17. Hiraoka, Y. & Sugai, S. (1985). Equilibrium and kinetic study of sodium- and potassium-induced conformational changes of apo-α-lactalbumin. Int. J. Pept. Protein Res. 26, 252-261.
18. Hiraoka, Y., Segawa, T., Kuwajima, K., Sugai, S. & Murai, N. (1980). α-Lactalbumin: a calcium metalloprotein. Biochem. Biophys. Res. Commun. 95, 1098-1104.
19. Horowitz, P. M., Hua, S. & Gibbons, D. L. (1995). Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomer or by ionic perterbation of the oligomer. J. Biol. Chem. 270, 1535-1542.
20. Ikeguchi, M., Kuwajima, K., Mitani, M. & Sugai, S. (1986). Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry, 25, 6965-6972.
21. Ito, K. & Akiyama, Y. (1991). In vivo analysis of integration of membrane proteins in Escherichia coli. Mol. Microbiol. 5, 2243-2253.
22. Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and consequences of GroEL-protein interactions. Biochemistry, 34, 14581-14587.
23. Katsumata, K., Okazaki, A. & Kuwajima, K. (1996). Effect of GroEL on the refolding kinetics of α-lactalbumin. J. Mol. Biol. 258, 827-838.
24. Kim, P. S. & Baldwin, R. L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
25. Kuwajima, K. (1996). The molten globule state of α-lactalbumin. FASEB J. 10, 102-109.
26. 2+ binding on the folding kinetics of α-lactalbumin. J. Mol. Biol. 206, 547-561.
27. Landry, S. J. & Gierasch, L. M. (1991). The chaperonin GroEL binds a polypeptide in an α-helical conformation. Biochemistry, 30, 7359-7362.
28. Landry, S. J. & Gierasch, L. M. (1994). Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu. Rev. Biophys. Biomol. Struct. 23, 645-669.
29. Landry, S. J., Jordan, R., McMacken, R. & Gierasch, L. M. (1992). Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature, 355, 455-457.
30. Lin, Z., Schwarz, F. P. & Eisenstein, E. (1995). The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 270, 1011-1014.
31. Lorimer, G. H. (1996). A quantitative assessment of the role of chaperonin proteins in protein folding in vivo. FASEB J. 10, 5-9.
32. Mayhew, M., Da Silva, A. C. R., Martin, J., Erdjument-Bromage, H., Tempst, P. & Hartl, F. U. (1996). Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature, 379, 420-426.
33. McKenzie, H. A. & White, F. H., Jr (1991). Lysozyme and α-lactalbumin: structure, function, and interrelationships. Advan. Protein Chem. 41, 173-315.
34. Mendoza, J. A., Rogers, E., Lorimer, G. H. & Horowitz, P. M. (1991). Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem. 266, 13044-13049.
35. Nall, B. T. (1994). Proline isomerization as a rate-limiting-step. In Mechanisms of Protein Folding (Pain, R. H., ed.), pp. 80-103, Oxford University Press Inc., Oxford.
36. Okazaki, A., Ikura, T., Nikaido, K. & Kuwajima, K. (1994). The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nature Struct. Biol. 1, 439-446.
37. Permyakov, E. A., Morozova, L. A. & Burstein, E. A. (1985). Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbumin. Biophys. Chem. 21, 21-31.
38. Privalov, P. L. & Gill, S. J. (1988). Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39, 191-234.
39. Robinson, C. V., Gross, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Hartl, F. U., Dobson, C. M. & Radford, S. E. (1994). Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature, 372, 646-651.
40. Rosenberg, H. F., Ackerman, S. J. & Tenen, D. G. (1993). Characterization of a distinct binding site for the prokaryotic chaperone, GroEL, on a human granulocyte ribonuclease. J. Biol. Chem. 268, 4499-4503.
41. Saibil, H. R., Zheng, D., Roseman, A. M., Hunter, A. S., Watson, G. M. F., Chen, S., Auf der Mauer, A., O'Hara, B. P., Wood, S. P., Mann, N. H., Barnett, L. K. & Ellis, R. J. (1993). ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr. Biol. 3, 265-273.
42. Spolar, R. S., Ha, J. H. & Record, M. T., Jr (1989). Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc. Natl Acad. Sci. USA, 86, 8382-8385.
43. Sturtevant, J. M. (1977). Heat capacity and entropy changes in processes involving proteins. Proc. Natl Acad. Sci. USA, 74, 2236-2240.
44. Sugai, S. & Ikeguchi, M. (1994). Conformational comparison between α-lactalbumin and lysozyme. Advan. Biophys. 30, 37-84.