The structural basis of yeast prion strain variants

Nature

Volumn 449, Issue 7159, 2007, Pages 233-237

  Toyama, Brandon H ^a   Kelly, Mark J S ^b   Gross, John D ^b   Weissman, Jonathan S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLOID; PEPTIDE;

AMINO ACID; BODY SHAPE; CRYSTALLOGRAPHY; PATHOGEN; PHENOTYPE; PRION DISEASE; PROTEIN; YEAST;

ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; DEUTERIUM HYDROGEN EXCHANGE; MUTAGENESIS; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRION; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY; YEAST;

EID: 34548615995     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06108     Document Type: Article

References (37)

1. Cohen, F. E. & Prusiner, S. B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67, 793-819 (1998).
2. 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).
3. Tuite, M. F. & Cox, B. S. The [PSI+] prion of yeast: a problem of inheritance. Methods 39, 9-22 (2006).
4. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
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. Nelson, R. et al. Structure of the cross-β spine of amyloid-like fibrils. Nature 435, 773-778 (2005).
7. Sawaya, M. R. et al. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 447, 453-457 (2007).
8. Tanaka, M., Collins, S. R., Toyama, B. H. & Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585-589 (2006).
9. Glover, J. R. et al. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89, 811-819 (1997).
10. Sparrer, H. E., Santoso, A., Szoka, F. C. Jr & Weissman, J. S. Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein. Science 289, 595-599 (2000).
11. King, C. Y. & Diaz-Avalos, R. Protein-only transmission of three yeast prion strains. Nature 428, 319-323 (2004).
12. Krishnan, R. & Lindquist, S. L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772 (2005).
13. Shewmaker, F., Wickner, R. B. & Tycko, R. Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure. Proc. Natl Acad. Sci. USA 103, 19754-19759 (2006).
14. Liu, J. J., Sondheimer, N. & Lindquist, S. L. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion. Proc. Natl Acad. Sci. USA [PSI+] 99 (suppl. 4), 16446-16453 (2002).
15. Flaux, J., Bertelsen, E. B., Horwich, A. L. & Wuthrich, K. NMR analysis of a 900K GroEL-GroES complex. Nature 418, 207-211 (2002).
16. Hoshino, M. et al. Mapping the core of the b2-microglobulin amyloid fibril by H/D exchange. Nature Struct. Biol. 9, 332-336 (2002).
17. 2-microglobulin amyloid fibrils as revealed by H/D exchange. J. Mol. Biol. 338, 559-571 (2004).
18. Ritter, C. et al. Correlation of structural elements and infectivity of the HET-s prion. Nature 435, 844-848 (2005).
19. Luhrs, T. et al. 3D structure of Alzheimer's amyloid-β(1-42) fibrils. Proc. Natl Acad. Sci. USA 102, 17342-17347 (2005).
20. Carulla, N. et al. Molecular recycling within amyloid fibrils. Nature 436, 554-558 (2005).
21. Chien, P., DePace, A. H., Collins, S. R. & Weissman, J. S. Generation of prion transmission barriers by mutational control of amyloid conformations. Nature 424, 948-951 (2003).
22. DePace, A. H. & Weissman, J. S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nature Struct. Biol. 9, 389-396 (2002).
23. Ross, E. D., Edskes, H. K., Terry, M. J. & Wickner, R. B. Primary sequence independence for prion formation. Proc. Natl Acad. Sci. USA 102, 12825-12830 (2005).
24. Tessier, P. M. & Lindquist, S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 447, 556-561 (2007).
25. King, C. Y. Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J. Mol. Biol. 307, 1247-1260 (2001).
26. DePace, A. H., Santoso, A., Hillner, P. & Weissman, J. S. A critical role for aminoterminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241-1252 (1998).
27. Osherovich, L. Z., Cox, B. S., Tuite, M. F. & Weissman, J. S. Dissection and design of yeast prions. PLoS Biol. 2, E86 (2004).
28. Crist, C. G., Nakayashiki, T., Kurahashi, H. & Nakamura, Y. [PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104. Genes Cells 8, 603-618 (2003).
29. Parham, S. N., Resende, C. G. & Tuite, M. F. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20, 2111-2119 (2001).
30. Shkundina, I. S., Kushnirov, V. V., Tuite, M. F. & Ter-Avanesyan, M. D. The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants. Genetics 172, 827-835 (2006).
31. Santoso, A., Chien, P., Osherovich, L. Z. & Weissman, J. S. Molecular basis of a yeast prion species barrier. Cell 100, 277-288 (2000).
32. Muchmore, D. C., McIntosh, L. P., Russell, C. B., Anderson, D. E. & Dahlquist, F. W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177, 44-73 (1989).
33. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
34. Goddard, T. D. & Kneller, D. G. SPARKY 3.112, University of California, San Francisco (2006).
35. Sattler, M., Schleucher, J. & Griesinger, C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158 (1999).
36. 15N-HSQC peaks using high-resolution 3D HNcocaNH experiments with nonuniform sampling. J. Biomol. NMR 33, 43-50 (2005).
37. 2D NMR spectra by interactive graphics. J. Magn. Reson. 84, 627-633 (1989).