The peculiar nature of unfolding of the human prion protein

Protein Science

Volumn 13, Issue 3, 2004, Pages 586-595

  Baskakov, Ilia V ^a   Legname, Giuseppe ^c   Gryczynski, Zygmunt ^b   Prusiner, Stanley B ^b,c  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Amyloid fibrils; Conformational transition; Prion protein; Size exclusion chromatography; Unfolding intermediates

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; PRION PROTEIN; RECOMBINANT PROTEIN; TRYPTOPHAN; UREA;

ALPHA HELIX; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DENATURATION; ENERGY TRANSFER; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; TECHNIQUE; THERMODYNAMICS;

ALGORITHMS; AMYLOID; CHROMATOGRAPHY, GEL; CHYMOTRYPSIN; CIRCULAR DICHROISM; FLUORESCENT DYES; HEAT; HUMANS; PEPTIDE FRAGMENTS; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TIME FACTORS; UREA;

EID: 1342331870     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03457204     Document Type: Article

References (27)

1. Apetri, A.C., and Surewicz, W.K. 2002. Kinetic intermediate in the folding of human prion protein. J. Biol. Chem. 277: 44589-44592.
2. Arnold, J.E., Tipler, C., Laszlo, L., Hope, J., Landon, M., and Mayer, R.J. 1995. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176: 403-411.
3. Baskakov, I.V. and Bolen, D.W. 1998. Monitoring the sizes of denatured ensembles of Staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics. Biochemistry 37: 18010-18017.
4. Baskakov, I.V., Aagaard, C., Mehlhorn, I., Wille, H., Groth, D., Baldwin, M.A., Prusiner, S.B., and Cohen, F.E. 2000. Self-assembly of recombinant prion protein of 106 residues. Biochemistry 39: 2792-2804.
5. Baskakov, I.V., Legname, G., Prusiner, S.B., and Cohen, F.E. 2001. Filding of prion protein to its native α-helical conformation is under kinetic control. J. Biol. Chem. 276: 19687-19690.
6. Baskakov, I.V., Legname, G., Baldwin, M.A., Prusiner, S.B., and Cohen, F.E. 2002. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 277: 21140-21148.
7. Bolen, D.W., and Yang, M. 2000. Effects of guanidine hydrochloride on the proton inventory of proteins: Implications on interpretations of protein stability. Biochemistry 39: 15208-15216.
8. Calzolai, L. and Zahn, R. 2003. Influence of pH on NMR structure and stability of the human prion protein globular domain. J. Biol. Chem. 278: 35592-35596.
9. Cohen, F.E. and Prusiner, S.B. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67: 793-819.
10. Hornemann, S. and Glockshuber, R. 1998. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl. Acad. Sci. 95: 6010-6014.
11. Hosszu, L.L.P., Baxter, A., Jackson, G.S., Power, A., Clarke, A.R., Waltho, J.P., Craven, C.J., and Collinge, J. 1999. Structural mobility of the human prion protein probed by backbone hydrogen exchange. Nat. Struct. Biol. 6: 740-743.
12. Kuwata, K., Li, H., Yamada, H., Legname, G., Prusiner, S.B., Akasaka, K., and James. T.L. 2002. Locally disordered conformer of the hamster prion protein: A crucial intermediate of PrPSc? Biochemistry 41: 12277-12283.
13. Lu, B.Y. and Chang, J.Y. 2001. Isolation of isoforms of mouse prion protein with PrPSc-like structural properties. Biochemistry 40: 13390-13396.
14. McKinley, M.P., Taraboulos, A., Kenaga, L., Serban, D., DeArmond, S.J., Stieber, A., and Prusiner, S.B. 1990. Ultrastructural localization of scrapie prion proteins in secondary lysosomes of infected cultured cells. J. Cell Biol. 111: 316a.
15. Mehlhorn, I., Groth, D., Stöckel, J., Moffat, B., Reilly, D., Yansura, D., Willett, W.S., Baldwin, M., Fletterick, R., Cohen, F.E., et al. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35: 5528-5537.
16. Morillas, M., Vanik, D.L., and Surewicz, W.K. 2001. On the mechanism of α-helix to β-sheet transition in the recombinant prion protein. Biochemistry 40: 6982-6987.
17. Nicholson, E.M., Mo, H., Prusiner, S.B., Cohen, F.E., and Marqusee, S. 2002. Differences between the prion protein and its homolog doppel: A partially structured state with implications for scrapie formation. J. Mol. Biol. 316: 807-815.
18. Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R.J., Cohen, F.E., et al. 1993. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. 90: 10962-10966.
19. Prusiner, S.B. 2001. Shattuck lecture-Neurodegenerative diseases and prions. N. Engl. J. Med. 344: 1516-1526.
20. Rezaei, H., Choiset, Y., Eghiaian, F., Treguer, E., Mentre, P., Debey, P., Grosclaude, J., and Haertle, T. 2002. Amyloidogenic unfolding intermediates differentiate sheep prion protein variants. J. Mol. Biol. 322: 799-814.
21. Safar, J., Roller, P.P., Gajdusek, D.C., and Gibbs Jr., C.J. 1994. Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33: 8375-8383.
22. Santoro, M.M. and 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.
23. Sokolowski, F., Modler, A.J., Masuch, R., Zirwer, D., Baier, M., Lutsch, G., Moss, D.A., Gast, K., and Naumann, D. 2003. Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein. J. Biol. Chem. [Epub ahead of print].
24. Swietnicki, W., Petersen, R., Gambetti, P., and Surewicz, W.K. 1997. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272: 27517-27520.
25. Wildegger, G., Liemann, S., and Glockshuber, R. 1999. Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat. Struct. Biol. 6: 550-553.
26. Yang, M., Liu, D., and Bolen, D.W. 1999. The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: A calorimetric study. Biochemistry 38: 11216-11222.
27. Zhang, H., Stöckel, J., Mehlhorn, I., Groth, D., Baldwin, M.A., Prusiner, S.B., James, T.L., and Cohen, F.E. 1997. Physical studies of conformational plasticity in a recombinant prion protein. Biochemistry 36: 3543-3553.