Amyloid formation of a yeast prion determinant

Journal of Molecular Neuroscience

Volumn 23, Issue 1-2, 2004, Pages 13-22

  Scheibel, Thomas ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Neurodegenerative disease; PrP; Sup35p; TSE; Yeast prion

Indexed keywords

AMYLOID; PRION PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE;

BIOCHEMISTRY; CORRELATION ANALYSIS; DISEASE TRANSMISSION; EPIGENETICS; GENE MUTATION; HYPOTHESIS; NONHUMAN; PRION; PRION DISEASE; PROTEIN DETERMINATION; PROTEIN FUNCTION; REVIEW; SACCHAROMYCES CEREVISIAE; YEAST; ANIMAL; BIOLOGICAL MODEL; BIOSYNTHESIS; GENETIC EPIGENESIS; GENETICS; HUMAN; METABOLISM;

MAMMALIA; SACCHAROMYCES CEREVISIAE;

AMYLOID; ANIMALS; EPIGENESIS, GENETIC; HUMANS; MODELS, BIOLOGICAL; PRION DISEASES; PRIONS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 4344701213     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/jmn:23:1-2:013     Document Type: Review

References (60)

1. Balbirnie M., Grothe R., and Eisenberg, D. S. (2001) An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA 98, 2375-2380.
2. Blake C. and Serpell L. (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure 4, 989-998.
3. Carrell R. and Lomas D. (1997) Conformational disease. Lancet 350, 134-138.
4. Chernoff Y. O., Derkatch I. L., and Inge-Vechtomov S. G. (1993) Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24, 268-270.
5. Chernoff Y. O., Galkin A. P., Lewitin E., Chernova T. A., Newnam G. P., and Belenkiy S. M. (2000) Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein. Mol. Microbiol. 35, 865-876.
6. Chiesa R., Piccardo P., Ghetti B., and Harris D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351.
7. DePace A. H. and Weissman J. S. (2002) Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat. Struct. Biol. 9, 389-396.
8. Derkatch I. L., Chernoff Y. O., Kushnirov V. V., Inge-Vechtomov S. G., and Liebman S. W. (1996) Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144, 1375-1386.
9. Dobson C. M. (2001) Protein folding and its links with human disease. Biochem. Soc. Symp. 68, 1-26.
10. Doel S. M., McCready S. J., Nierras C. R., and Cox B. S. (1994) The dominant PNM2- mutation which eliminates the PSI factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137, 659-670.
11. Eaglestone S. S., Cox B. S., and Tuite M. F. (1999) Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18, 1974-1981.
12. Esler W. P., Felix A. M., Stimson E. R., Lachenmann M. J., Ghilardi J. R., Lu Y. A., et al. (2000) Activation barriers to structural transition determine deposition rates of Alzheimer's disease a beta amyloid. J. Struct. Biol. 130, 174-183.
13. Frolova L., Le Goff X., Zhouravleva G., Davydova E., Philippe M., and Kisselev L. (1996) Eukaryotic polypeptide chain release factor eRF3 is an eRF1-and ribosome-dependent guanosine triphosphatase. RNA 2, 334-341.
14. Geddes A. J., Parker K. D., Atkins E. D., and Beighton E. (1968) "Cross-beta" conformation in proteins. J. Mol. Biol. 32, 343-358.
15. Glover J. R., Kowal A. S., Schirmer E. C., Patino M. M., Liu J. J., and Lindquist S. (1997) Self-seeded fibers formed by Sup35p, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89, 811-819.
16. Griffith J. S. (1967) Self-replication and scrapie. Nature 215, 1043-1044.
17. Hammarstrom P., Wiseman R. L., Powers E. T., and Kelly J. W. (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299, 713-716.
18. Harper J. D., Wong S. S., Lieber C. M., and Lansbury P. T. (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
19. Inoue Y., Kishimoto A., Hirao J., Yoshida M., and Taguchi H. (2001) Strong growth polarity of yeast prion fiber revealed by single fiber imaging. J. Biol. Chem. 276, 35227-35230.
20. Jarrett J. T., Berger E. P., and Lansbury P. T. (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697.
21. Kelly J. W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6, 11-17.
22. Kelly J. W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106.
23. King C. Y., Tittmann P., Gross H., Gebert R., Aebi M., and Wuthrich K. (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. USA 94, 6618-6622.
24. Koo E. H., Lansbury P. T., and Kelly J. W. (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. USA 96, 9989-9990.
25. Kushnirov V. V., Kryndushkin D. S., Boguta M., Smirnov V. N., and Ter-Avanesyan M. D. (2000) Chaperones that cure yeast artificial [PSI+] and their prion-specific effects. Curr. Biol. 10, 1443-1446.
26. Kushnirov V. V., Ter-Avanesyan M. D., Surguchov A. P., Smirnov V. N., and Inge-Vechtomov S. G. (1987) Localization of possible functional domains in sup2 gene product of the yeast Saccharomyces cerevisiae. FEBS Lett. 215, 257-260.
27. Kushnirov V. V., Ter-Avanesyan M. D., Telckov M. V., Surguchov A. P., Smirnov V. N., and Inge-Vechtomov S. G. (1988) Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae. Gene 66, 45-54.
28. Liebman S. W. and Derkatch I. L. (1999) The yeast [PSI+] prion: making sense of nonsense. J.Biol.Chem.274, 1181-1184.
29. Liu J. J. and Lindquist S. (1999) Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400, 573-576.
30. Lomakin A., Teplow D. B., Kirschner D. A., and Benedek G. B. (1997) Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc. Natl. Acad. Sci. USA 94, 7942-7947.
31. Masel J. and Jansen V. A. (2000) Designing drugs to stop the formation of prion aggregates and other amyloids. Biophys. Chem. 88, 47-59.
32. Massi F. and Straub J. E. (2001) Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation. Proteins 42, 217-229.
33. Merlini G., Bellotti V., Andreola A., Palladini G., Obici L., Casarini S., and Perfetti V. (2001) Protein aggregation. Clin. Chem. Lab. Med. 39, 1065-1075.
34. Partridge L. and Barton N. H. (2000) Evolving evolvability. Nature 407, 457, 458.
35. Parham S. N., Resende C. G., and Tuite M. F. (2001) Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20, 2111-2119.
36. Patino M. M., Liu J. J., Glover J. R., and Lindquist S. (1996) Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
37. Paushkin S. V., Kushnirov V. V., Smirnov V. N., and Ter-Avanesyan M. D. (1996) Propagation of the yeast prion-like [PSI+] determinant is mediated by oligomerization of the SUP35P-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134.
38. Paushkin S. V., Kushnirov V. V., Smirnov V. N., and Ter-Avanesyan M. D. (1997) In vitro propagation of the prion-like state of yeast Sup35 protein. Science 277, 81-383.
39. Prusiner S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144.
40. Prusiner S. B. (1997) Prion diseases and the BSE crisis. Science 278, 245-251.
41. Prusiner S. B. (1998) Prions. Proc. Natl. Acad. Sci. USA 95, 13363-13383.
42. Prusiner S. B. and Scott, M. R. (1997) Genetics of prions. Annu. Rev. Genet. 31, 139-175.
43. Rochet J. C. and Lansbury P. T. (2000) Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10, 60-68.
44. Santoso A., Chien P., Osherovich L. Z. and Weissman J. S. (2000) Molecular basis of a yeast prion species barrier. Cell 100, 277-288.
45. Scheibel T. and Lindquist S. (2001) The role of conformational flexibility in amyloid propagation by the yeast prion-protein Sup35. Nat. Struct. Biol. 8, 958-962.
46. Scheibel T., Bloom J., and Lindquist S. (2004) The elongation of yeast prion fibers involves separable steps of association and conversion. Proc. Natl. Acad. Sci. USA 101, 2287-2292.
47. Scheibel T., Kowal A., Bloom J., and Lindquist S. (2001) Bi-directional amyloid fiber growth for a yeast prion determinant. Curr. Biol. 11, 366-369.
48. Serio T. R. and Lindquist S. L. (1999) [PSI+]: an epigenetic modulator of translation termination efficiency. Annu. Rev. Cell Dev. Biol. 15, 661-703.
49. Serio T. R. and Lindquist S. L. (2000) Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol. 10, 98-105.
50. Serio T. R., Cashikar A. G., Kowal A. S., Sawicki G. J., Moslehi J. J., Serpell L., et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317-1321.
51. Sparrer H. E., Santoso A., Szoka F. C., and Weissman J. S. (2000) Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein. Science 289, 595-599.
52. Stansfield I., Jones K. M., Kushnirov V. V., Dagkesamanskaya A. R., Poznyakovski A. I., Paushkin S. V., et al. (1995) The products of the SUP45 (eRF1) and SUP35P genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365-4373.
53. Sunde M. and Blake C. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. Adv. Protein Chem. 50, 123-159.
54. Ter-Avanesyan M. D., Dagkesamanskaya A. R., Kushnirov V. V., and Smirnov V. N. (1994) The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 137, 671-676.
55. Ter-Avanesyan M. D., Kushnirov V. V., Dagkesamanskaya A. R., Didichenko S. A., Chernoff Y. O., Inge-Vechtomov S. G., and Smirnov V. N. (1993) Deletion analysis of the SUP35P gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683-692.
56. True H. and Lindquist S. (2000) A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477-485.
57. Weissmann C. (1999) Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274, 3-6.
58. Wickner R. B. (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569.
59. Wickner R. B., Taylor K. L., Edskes H. K., Maddelein M. L., Moriyama H., and Roberts B. T (2000) Prions of yeast as heritable amyloidoses. J. Struct. Biol. 130, 310-322.
60. Zhouravleva G., Frolova L., Le Goff X., Le Guellec R., Inge-Vechtomov S., Kisselev L., and Philippe M. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065-4072.