Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein

Journal of Molecular Biology

Volumn 261, Issue 5, 1996, Pages 614-619

  Hornemann, Simone ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Periplasmic expression in Escherichia coli; Prion protein; Protein folding; Protein stability; Proteolytic degradation

Indexed keywords

GUANIDINE; MUTANT PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; MOUSE; NONHUMAN; PRION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SOLUBILITY; THERMODYNAMICS;

EID: 0030572627     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0487     Document Type: Editorial

References (35)

1. Baker, D., Sohl, J. L. & Agard, D. A. (1992). A protein-folding reaction under kinetic control. Nature, 356, 263-265.
2. Baldwin, R. L. (1996). On-pathway versus off-pathway folding intermediates. Folding & Design, 1, R1-R8.
3. Büeler, H., Aguzzi, A., Sailer, A., Greiner, R. A., Autenried, P., Aguet, M. & Weissmann, C. (1993). Mice devoid of PrP are resistant to scrapie. Cell, 73, 1339-1347.
4. Collinge, J., Whittington, M. A., Sidle, K. C., Smith, C. J., Palmer, M. S., Clarke, A. R. & Jefferys, J. G. R. (1994). Prion protein is necessary for normal synaptic function. Nature, 370, 295-297.
5. de Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, G. F., Forloni, G., Tagliavini, F. & Salmona, M. (1994). Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J. Biol. Chem. 269, 7859-7862.
6. de Prat Gay, G., Ruiz-Sanz, J., Neira, J., Itzhaki, L. S. & Fersht, A. R. (1995a). Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module. Proc. Natl Acad. Sci. USA, 92, 3683-3686.
7. de Prat Gay, G., Ruiz-Sanz, J., Neira, J., Corrales, F. J., Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995b). Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. J. Mol. Biol. 254, 968-979.
8. Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A. & Wright, P. E. (1992). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226, 795-817.
9. 1: characterization of a folding intermediate. Biochemistry, 32, 18-26.
10. 1: role of the pro-sequence. Biochemistry, 32, 18-26.
11. Fischer, M., Rülicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., Brandner, S., Aguzzi, A. & Weissmann, C. (1996). Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15, 1255-1264.
12. Gill, S. C. & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
13. Griffith, J. S. (1967). Self-replication and scrapie. Nature, 215, 1043-1044.
14. Huang, Z., Gabriel, J.-M., Baldwin, M. A., Fletterick, R. J., Prusiner, S. B. & Cohen, F. E. (1994). Proposed three-dimensional structure for the cellular prion protein. Proc. Natl Acad. Sci. USA, 91, 7139-7143.
15. Huang, Z., Prusiner, S. B. & Cohen, F. E. (1995). Scrapie prions: a three-dimensional model of an infectious fragment. Folding Design, 1, 13-19.
16. Johnson, W. C., Jr (1990). Protein secondary structure and circular dichroism: practical guide. Proteins: Struct. Funct. Genet. 7, 205-214.
17. Kazmirski, S. L., Alonso, D. O. V., Cohen, F. E., Prusiner, S. B. & Daggett, V. (1995). Theoretical studies of the sequence effects on the conformational properties of a fragment of the prion protein: implications for scrapie formation. Chem. Biol. 2, 305-315.
18. Myers, J. K., Pace, C. N. & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
19. Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
20. Palmer, M. S., Dryden, A. J., Hughes, J. T. & Collinge, J. (1991). Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature, 352, 340-342.
21. Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., Cohen, F. E. & Prusiner, S. B. (1993). Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA, 90, 10962-10966.
22. Price, N. C. & Johnson, C. M. (1993). Proteinases as probes of conformation of soluble proteins. In Proteolytic Enzymes, A Practical Approach (Beynon, R. J. & Bond, J. S., eds), pp. 163-180, IRL Press, Oxford.
23. Prusiner, S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science, 216, 136-144.
24. Prusiner, S. B. (1991). Molecular biology of prion diseases. Science, 252, 1515-1522.
25. Prusiner, S. B. (1993). Genetic and infectious prion diseases. Arch. Neurol. 50, 1129-1153.
26. Safar, J., Roller, P. P., Gajdusek, D. C. & Gibbs, C. J., Jr (1994). Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry, 33, 8375-8383.
27. Santoro, M. M. & Bolen, D. W. (1988). Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry, 27, 8063-8068.
28. Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Katoaka, Y., Houtani, T., Shirabe, S., Okada, H., Hasegawa, S., Miyamoto, T. & Noda, T. (1996). Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature, 380, 528-531.
29. Schätzl, H. M., Da Costa, M., Taylor, L., Cohen, F. E. & Prusiner, S. B. (1995). Prion protein gene variation among primates. J. Mol. Biol. 245, 362-374.
30. Stahl, N. & Prusiner, S. B. (1991). Prions and prion proteins. FASEB J. 5, 2799-2807.
31. Strobl, S., Mühlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockshuber, R. & Holak, T. A. (1995). Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from Ragi seeds by NMR-spectroscopy. Biochemistry, 34, 8281-8293.
32. Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
33. Weissmann, C. (1994). Molecular biology of prion diseases. Trends Cell Biol. 4, 10-14.
34. Weissmann, C. (1995). Yielding under the strain. Nature, 375, 620-628.
35. Westaway, D., Goodman, P. A., Mirenda, C. A., McKinely, M. P., Carlson, G. A. & Prusiner, S. B. (1987). Distinct prion proteins in short and long scrapie incubation period mice. Cell, 51, 651-662.