The physical basis of how prion conformations determine strain phenotypes

Nature

Volumn 442, Issue 7102, 2006, Pages 585-589

  Tanaka, Motomasa ^a,b   Collins, Sean R ^a   Toyama, Brandon H ^a   Weissman, Jonathan S ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

PATHOLOGY; PHYSIOLOGY; PROTEINS; YEAST;

DYNAMIC INTERACTION; PHYSIOLOGICAL IMPACT; PRION CONFORMATION;

CONFORMATIONS;

AMYLOID;

AGGREGATION; MAMMAL; PHENOTYPE; PROTEIN; YEAST;

ARTICLE; CELL DIVISION; GROWTH; NONHUMAN; PHENOTYPE; PRION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; STRAIN DIFFERENCE; STRAIN IDENTIFICATION; YEAST;

MAMMALIAN PRION;

EID: 33746698975     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04922     Document Type: Article

References (30)

1. Caughey, B. & Lansbury, P. T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298 (2003).
2. Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
3. Collinge, J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519-550 (2001).
4. King, C. Y. & Diaz-Avalos, R. Protein-only transmission of three yeast prion strains. Nature 428, 319-323 (2004).
5. Tanaka, M., Chien, P., Naber, N., Cooke, R. & Weissman, J. S. Conformational variations in an infectious protein determine prion strain differences. Nature 428, 323-328 (2004).
6. Legname, G. et al. Synthetic mammalian prions. Science 305, 673-676 (2004).
7. Brachmann, A., Baxa, U. & Wickner, R. B. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J. 24, 3082-3092 (2005).
8. Wickner, R. B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569 (1994).
9. Tuite, M. F. & Koloteva-Levin, N. Propagating prions in fungi and mammals. Mol. Cell 14, 541-552 (2004).
10. Shorter, J. & Lindquist, S. Prions as adaptive conduits of memory and inheritance. Nature Rev. Genet. 6, 435-450 (2005).
11. Derkatch, I. L., Chernoff, Y. O., Kushnirov, V. V., Inge-Vechtomov, S. G. & Liebman, S. W. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144, 1375-1386 (1996).
12. +] prion generation in yeast: characterization of the 'strain' difference. Yeast 18, 489-497 (2001).
13. Kushnirov, V. V. & Ter-Avanesyan, M. D. Structure and replication of yeast prions. Cell 94, 13-16 (1998).
14. Bradley, M. E., Edskes, H. K., Hong, J. Y., Wickner, R. B. & Liebman, S. W. Interactions among prions and prion "strains" in yeast. Proc. Natl Acad. Sci. USA 99 (suppl. 4), 16392-16399 (2002).
15. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278, 49636-49643 (2003).
16. Castilla, J., Saa, P., Hetz, C. & Soto, C. In vitro generation of infectious scrapie prions. Cell 121, 195-206 (2005).
17. Krishnan, R. & Lindquist, S. L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772 (2005).
18. +] prion in yeast. Genetics 165, 23-33 (2003).
19. Collins, S. R., Douglass, A., Vale, R. D. & Weissman, J. S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2, e321 (2004).
20. Satpute-Krishnan, P. & Serio, T. R. Prion protein remodelling confers an immediate phenotypic switch. Nature 437, 262-265 (2005).
21. DePace, A. H. & Weissman, J. S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nature Struct. Biol. 9, 389-396 (2002).
22. Ness, F., Ferreira, P., Cox, B. S. & Tuite, M. F. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol. Cell. Biol. 22, 5593-5605 (2002).
23. Masel, J., Jansen, V. A. & Nowak, M. A. Quantifying the kinetic parameters of prion replication. Biophys. Chem. 77, 139-152 (1999).
24. Weissmann, C. The state of the prion. Nature Rev. Microbiol. 2, 861-871 (2004).
25. Hall, D. & Edskes, H. Silent prions lying in wait: a two-hit model of prion/amyloid formation and infection. J. Mol. Biol. 336, 775-786 (2004).
26. Tanaka, M., Chien, P., Yonekura, K. & Weissman, J. S. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121, 49-62 (2005).
27. +] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol. Microbiol. 40, 1357-1369 (2001).
28. Jung, G. & Masison, D. C. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol. 43, 7-10 (2001).
29. Silveira, J. R. et al. The most infectious prion protein particles. Nature 437, 257-261 (2005).
30. Santoso, A., Chien, P., Osherovich, L. Z. & Weissman, J. S. Molecular basis of a yeast prion species barrier. Cell 100, 277-288 (2000).