Hydrogen-exchange kinetics of reduced α-lactalbumin bound to the chaperonin GroEL

Journal of Biochemistry

Volumn 121, Issue 3, 1997, Pages 534-541

  Okazaki, Akira ^a   Katsumata, Kumiko ^a   Kuwajima, Kunihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Chaperonin; GroEL; Hydrogen exchange; Molecular chaperone; lactalbumin

Indexed keywords

CHAPERONIN; LACTALBUMIN;

ARTICLE; BIOCHEMISTRY; CIRCULAR DICHROISM; DISULFIDE BOND; MASS SPECTROMETRY; NONHUMAN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT;

EID: 0030992101     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021619     Document Type: Article

References (41)

1. Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45
2. Ellis, R.J. and Hartl, F.-U. (1996) Protein folding in the cell: competing models of chaperonin function. FASEB J. 10, 20-26
3. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D.C., Joachimiak, A., Norwich, A.L., and Sigler, P.B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371, 578-586
4. Braig, K., Adams, P.D., and 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. Weissman, J.S., Hohl, C.M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K., Saibil, H.R., Fenton, W.A., and Horwich, A.L. (1995) Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-587
6. Weissman, J.S., Rye, H.S., Fenton, W.A., Beechem, J.M., and Horwich, A.L. (1996) Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490
7. Mayhew, M., Silva, A.C.R., Martin, J., Erdjument-Bromage, H., Tempst, P., and Hartl, F.U. (1996) Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379, 420-426
8. Lin, Z., Schwarz, F.P., and Eisenstein, E. (1995) The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 270, 1011-1014
9. Katsumata, K., Okazaki, A., Tsurupa, G.P., and Kuwajima, K. (1996) Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J. Mol. Biol. 264, 643- 649
10. Zahn, R., Axmann, S.E., Rücknagel, K., Jaeger, E., Laminet, A. A., and Plückthun, A. (1994) Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of β-lactamase precursor. J. Mol. Biol. 242, 150-164
11. Zahn, R. and Plückthun, A. (1994) Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase. J. Mol. Biol. 242, 165-174
12. Landry, S.J. and Gierasch, L.M. (1991) The chaperonin GroEL binds a polypeptide in an α-helical conformation. Biochemistry 30, 7359-7362
13. Landry, S.J., Jordan, R., McMacken, R., and Gierasch, L.M. (1992) Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature 355, 455-457
14. Schmidt, M. and Buchner, J. (1992) Interaction of GroE with an all-β-protein. J. Biol. Chem. 267, 16829-16833
15. Hayer-Hartl, M.K., Ewbank, J.J., Creighton, T.E., and Hartl, F.U. (1994) Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin. EMBO J. 13, 3192-3202
16. Robinson, C.V., Groß, M., Eyles, S.J., Ewbank, J.J., Mayhew, M., Hartl, F.U., Dobson, C.M., and Radford, S.E. (1994) Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature 372, 646-651
17. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L., and Hartl, F.-U. (1991) Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate. Nature 352, 36-42
18. Katsumata, K., Okazaki, A., and Kuwajima, K. (1996) Effect of GroEL on the re-folding kinetics of α-lactalbumin. J. Mol. Biol. 258, 827-838
19. Okazaki, A., Ikura, T., Nikaido, K., and Kuwajima, K. (1994) The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nature Struct. Biol. 1, 439-446
20. Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K., and Plückthun, A. (1994) Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368, 261- 265
21. Zahn, R., Perrett, S., Stenberg, G., and Fersht, A.R. (1996) Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science 271, 642-645
22. Zahn, R., Perrett, S., and Fersht, R. (1996) Conformational states bound by the molecular chaperones GroEL and SecB: a hidden unfolding (annealing) activity. J. Mol. Biol. 261, 43-61
23. Todd, M.J., Viitanen, P.V., and Lorimer, G.H. (1994) Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265, 659-666
24. 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
25. Ito, K. and Akiyama, Y. (1991) In vivo analysis of integration of membrane proteins in Escherichia coli, Mol. Microbiol. 5, 2243- 2253
26. Kuwajima, K., Nitta, K., Yoneyama, M., and Sugai, S. (1976) Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106, 359-373
27. Hiraoka, Y., Segawa, T., Kuwajima, K., Sugai, S., and Murai, N. (1980) α-Lactalbumin: a calcium metalloprotein. Biochem. Biophys. Res. Commun. 95, 1098-1104
28. Ikeguchi, M. and Sugai, S. (1989) Contribution of disulfide bonds to stability of the folding intermediate of α-lactalbumin. Int. J. Pept. Protein Res. 33, 289-297
29. Ikeguchi, M., Sugai, S., Fujino, M., Sugawara, T., and Kuwajima, K. (1992) Contribution of the 6-120 disulfide bond of α- lactalbumin to the stabilities of its native and molten globule states. Biochemistry 31, 12695-12700
30. Jentoft, N. and Dearborn, D.G. (1979) Labeling of proteins by reductive methylation using sodium cyanoborohydride. J. Biol. Chem. 254, 4359-4365
31. Greenfield, N.J. and Fasman, G.D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116
32. Saxena, V.P. and Wetlaufer, D.B. (1971) A new basis for interpreting the circular dichroic spectra of proteins. Proc. Natl. Acad. Sci. USA 68, 969-972
33. Chen, Y.H., Yang, J.T., and Chau, K.H. (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359
34. Ellman, G.L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77
35. Riddles, P.W., Blakeley, R.L., and Zerner, B. (1979) Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - a reexamination. Anal. Biochem. 94, 75-81
36. Englander, S.W., Sosnick, T.R., Englander, J.J., and Mayne, L. (1996) Mechanisms and uses of hydrogen exchange. Curr. Opin. Struct. Biol. 6, 18-23
37. Englander, S.W. and Kallenbach, N.R. (1984) Hydrogen ex- change and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-655
38. Hlodan, R., Tempst, P., and Hartl, F.U. (1995) Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding. Nature Struct. Biol. 2, 587-595
39. Kyte, J. and Doolittle, R.F. (1982) A simple method for display- ing the hydropathic character of a protein. J. Mol. Biol. 157, 105- 132
40. Peng, Z.-Y. and Kim, P.S. (1994) A protein dissection study of a molten globule. Biochemistry 33, 2136-2141
41. Schulman, B.A. and Kim, P.S. (1996) Prorene scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. Nature Struct. Biol. 3, 682-687