Analytical background and discussion of the chaperone model of prion diseases

Acta Biotheoretica

Volumn 47, Issue 3-4, 1999, Pages 219-238

  Liautard, J P ^a  

^a INSERM   (France)

Author keywords

Chaperone; Folding; Irreversible thermodynamics; Multiple structures

Indexed keywords

ANIMALIA; SCRAPIE PRION;

EID: 0033509065     PISSN: 00015342     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1002642821806     Document Type: Conference Paper

References (54)

1. Anfinsen, C. (1973). Principles that govern the folding of proteins chains. Science 18: 223-230.
2. Baker, D., J. Sohl and D.A. Agard (1992). A protein-folding reaction under kinetic control. Nature 356: 263-265.
3. Bastiras, S. and J.C. Wallace (1992). Equilibrium Denaturation of recombinant porcine growth hormaone. Biochemistry 31: 9304-9309.
4. Bessen, R., D.A. Kocisko, G.J. Raymond, S. Nandan, P.T. Lansbury and B. Caughey (1995). Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375: 698-700.
5. Brandt-Kauf, P.W., R. Monaco and M.R. Pincus (1994). Conformational effects of environementally induced cancer-related mutations in the p53 protein. Proceedings of the National Academy of Science USA 91: 9262-9266.
6. Brooks, C., M. Karplus and M. Pettitt (1989) Proteins: a theoritical perspective of dynamics, structure, and thermodynamics. John Wiley & Son, New York.
7. Bycroft, M., A. Matouschek, J.T. Kellis, L. Serano and A.R. Fersht (1990). Detection and characterization of a folding intermediate in barnase by RMN. Nature 346: 488-490.
8. Caughey, B., D. A. Kocisko, G.J. Raymond and P.T. Lansburry (1996). Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Current Biology 2: 807-817.
9. Caughey, B.W., A. Dong, K. Bhat, D. Ernst, S. Hayes and W.S Caughey (1991). Secondary structure analysis of the scrapie-associated PrP 27-30 in water by infrared spectroscopy. Biochemistry 30: 7672-7680.
10. Cheng, M.Y., F. U. Hartl and A.L. Horwich. (1990). The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348: 455-458.
11. Chothia, C. and A.V. Finkelstein (1990). The classification and origins of protein folding patterns. Annual Review of Biochemistry 59: 1007-1039.
12. Chou, P. and G. Fasman (1978). Prediction of the secondary structure of proteins from thier amino acid sequence. Advance in Enzymology 47: 45-148.
13. Cohen, F.E., K.M. Pan, Z. Huang., M. Baldwin, R.J. Fletterick and S.B. Prusiner (1994). Structural clues to prion replication. Science 264: 530-531.
14. Come, J.H., P.E. Fraser and P.T. Lansbury. (1993). A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proceeding of the National Academy of Science USA 90: 5959-5963.
15. Elis, J.R. and S.M. van der Vies (1991). Molecular chaperones. Annual Review of Biochemistry 60: 321-347.
16. Elis, R. J. (1987). Proteins as molecular chaperones. Nature 328: 378-379.
17. Ferraz, C., F. Heitz, J. SriWidada, E. Caron, A. Cave and J.P. Liautard. (1991). Conformational stability of human skeletal tropomyosins modified by site-directed mutagenesis. Protein Engineering 4: 561-568.
18. Garnier, J., D.J. Osguthorpe, and B. Robson. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology 120: 97-120.
19. Ghelis, C. and J. Yon (1982). Protein Folding. Academic Press, New York.
20. Goldberg, M. E. (1972). Dynamic Aspects of Conformation Changes in Biological Molecules. Dordrecht, Netherlands, Reidl Publ.
21. Hupp, T.R. and D.P. Lane (1994). Allosteric activation of latent p53 tetramers. Current Biology 4: 865-875.
22. Jarrett, J. T. and P. T. Lansbury (1993). Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer disease and scrapie. Cell 73: 1055-1058.
23. Jou, D. and J.E. Llebot (1991). Introduction a la thermodynamique des processus bioilogiques. Paris, Techniques & Documentation-Lavoisier; Harper & Row.
24. Katchalsky, A. and P.F. Curran (1965). Nonequilibrium Thermodynamics in Biophysics. Cambridge Massachussets, Harvard University Press,.
25. Kim, P.S. and R.L. Baldwin (1990). Intermediates in the folding reactions of small proteins. Annual Review of Biochemistry 59: 631-660.
26. Landry, S.J. and L.M. Gierasch (1991). The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry 307: 359-362.
27. Landry, S.J., R. Jordan, R. McMachen and L. Gierash. (1992). Different conformation for the same polypeptide bound the chaperone DnaK and GroEL. Nature 355: 455-457.
28. Lattman, E. E. and G.D. Rose (1993). Protein folding-What's the question? Proceeding of the National Academy of Science USA 90: 439-441.
29. Liautard, J.P. (1990). Approche thermocinètique du repliement des protèines. Compte Rendu de l'Académie des Sciences 311: 385-389.
30. Liautard, J.P. (1991). Are prions misfolded molecular chaperones? Federation of European Biochemical Societies Letters 294: 155-157.
31. Liautard, J.P. (1993). Anew theoritical model of protein folding could explain the ethiology of degenerative encephalopathy. Biologie prospective. Editeurs: Galteau M.M, Siest G. and J. Henny. John Libbey Eurotext, Paris: . pp 607-614, i.
32. London, J., C. Skrzynia and M. Goldberg. (1974). Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers. European Journal of Biochemistry 47: 409-415.
33. Martin, J., T. Langer, R. Boteva, A. Schramel, A. Horwich and F.-U. Hartl (1991). Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate. Nature 352: 36-42.
34. Matthews, R.C. (1991). The mechanism of protein folding. Current Opinion in Structural Biology 1: 28-35.
35. Milner, J. (1995). Flexibility: the key function to p53 function? Trends in Biochemical sciences 20: 49-51.
36. Mitraki, A., B. Fane, C. Haase, J. Strutevant and J. King. (1991). Global suppression of protein folding defects and inclusion body formation. Science 253: 54-58.
37. Pan, K., M. Baldwin, J. Nguyen, M. Gasset, A. Serban, D. Groth, I. Mehlhorn, Z. Huang, R.J. Fletterick, F.E. Cohen and S.B. Prusiner (1993). Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins. Proceedings of the National Academy of Science USA 90: 10962-10966.
38. Peralta, D., D.J. Hartman, N.J. Hoogenraad and P.B. Hoj (1994). Generation of a stable folding intermediate which can be rescued by the chaperonin GroEL and GroES. Federation of European Biochemical Societies Letters 339: 45-49.
39. Pinhasi, O., D. Michalovitz, A. Ben-Zeev and M. Oren. (1986). Specific interaction between th p53 cellular tumor antigen and the major heat shock proteins. Nature 320: 182-185.
40. Pititsyn, O. B., R. H. Pain, G.V. Semisotnov, E. Zerovnik and O.I. Razguliaev (1990). The molten globule. Federation of European Biochemical Societies Letters 262: 20-24.
41. Prigogine, I. (1968). Introduction à la thermodynamique des processus irreversibles. Paris, Dunod,.
42. Prusiner, S. (1991). Molecular Biology of prion diseases. Science 252: 1515-1522.
43. Safar, J., P.P. Roller, C. Gajdusek and C.J. Gibbs (1993). Conformational transition, dissociation and unfolding of scrapie amyloid (prion) protein. The Journal of Biological Chemistry 268: 20276-20284.
44. Schmid, F. X. (1991). Catalysis and assistance of protein folding. Current Opinion in Structural Biology 1: 36-41.
45. Serrano, L., A. Matouschek and A.R. Fersht (1992). The folding of an enzyme. VI The folding pathway of barnase: comparison with theoritical model. Journal of Molecular Biology 224: 847-859.
46. Shinde, U. P., J.J. Liu and M. Inouye (1997). Protein memory through altered folding mediated by intramolecular chaperones. Nature 389: 520-522.
47. Sippl, M. J. (1990). Calculation and conformational ensembles from potentials of a mean force. An approach to the knowledge-based prediction of local structures in globular proteins. Journal of Molecular Biology 213: 859-863.
48. Stahl, N., M.A. Baldwin, D.B. Teplow, L. Hood, B.W. Gibson, A.L. Burlingame and S.B. Prusiner (1993). Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32: 1991-2002.
49. Sugawara, T., K. Kuwajima and S. Sugai (1991). Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. Biochemistry 30: 2698-2706.
50. Tanford, C. (1967). In Physical Chemistry of macromolecules. New York., John Wiley & Son Inc.
51. Todd, M. J., P.V. Viitanen and G.H. Lorimer (1994). Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265: 659-666.
52. Viitanen, P.V., T.H. Lubben, P. Goloubinoff, P.O. O'Keefe and G.H. Lorimer. (1990). Chaperonin-facilited refolding of ribulose-bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (GroEL) are K+ -dependent. Biochemistry 29: 5665-5671.
53. Zhu, X., Y. Ohta, F. Jordan and M. Inouye (1989). Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339: 483-484.
54. Zimm, B.H. and J.K. Bragg (1959). Theory of the phase transition between helix and random coil in polypeptide chains. Journal of Chemical Physics 31: 526-532.