Skip to main content
SpringerLink
Log in

Prions of Yeast From Cytoplasmic Genes to Heritable Amyloidosis

  • Protocol
Molecular Pathology of the Prions

Part of the book series: Methods in Molecular Medicine™ ((MIMM,volume 59))

  • 522 Accesses

Abstract

It was believed that only proteins could carry out enzymatic reactions, and only nucleic acids could mediate inheritance. In recent years, the work of Cech and Altman and others has shown that nucleic acids can catalyze reactions. Now it has been shown that, in yeast, proteins can mediate inheritance. The infectious protein (prion) concept arose from studies of the transmissible spongiform encephalopathies (TSEs) of mammals (1), and several lines of evidence suggest that TSEs are indeed caused by infectious forms of the PrP protein, but the absence of definitive proof has left substantial doubt and disagreement on this point (2–6). The ease of genetic manipulation of yeast offers experimental possibilities not yet available even in the mouse system. This enabled the discovery of yeast prions (7), and has facilitated the rapid characterization of these systems. The parallels between the yeast and mammalian systems are striking. Moreover, because both of the yeast prion systems appear to involve self-propagating amyloid forms of the respective proteins, these systems may also serve as models for the broader class of diseases for which amyloid accumulation is a central feature. The discovery of the [HET-s] prion of the filamentous fungus Podospora, another genetically manipulable system, adds a new dimension to prion studies (8).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 159.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Griffith, J. S. (1967) Self-replication and scrapie. Nature 215, 1043–1044

    Article  PubMed  CAS  Google Scholar 

  2. Chesebro, B. (1998) BSE and prions: uncertainties about the agent. Science 279, 42–43

    Article  PubMed  CAS  Google Scholar 

  3. Farquhar, C. F., Somerville, R. A., and Bruce, M. E. (1998) Straining the prion hypothesis. Nature 391, 345–346

    Article  PubMed  CAS  Google Scholar 

  4. Prusiner, S. B. (1998) Prions. Proc. Natl. Acad. Sci. USA. 95, 13,363–13,383

    Article  CAS  Google Scholar 

  5. Manson, J. C., Jamieson, E., Baybutt, H., Tuzi, N. L., Barron, R., McConnell, I., et al. (1999) Single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy. EMBO J. 18, 6855–6864

    Article  PubMed  CAS  Google Scholar 

  6. Weissmann, C. (1999) Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274, 3–6

    Article  PubMed  CAS  Google Scholar 

  7. Wickner, R. B. (1994) Evidence for a prion analog in S. cerevisiae: the (URE3) nonMendelian genetic element as an altered URE2 protein. Science 264, 566–569

    Article  PubMed  CAS  Google Scholar 

  8. Coustou, V., Deleu, C., Saupe, S., and Begueret, J. (1997) Protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. USA 94, 9773–9778

    Article  PubMed  CAS  Google Scholar 

  9. Wickner, R. B., Masison, D. C., and Edskes, H. K. (1995) [PSI] and [URE3] as yeast prions. Yeast 11, 1671–1685

    Article  PubMed  CAS  Google Scholar 

  10. Lindquist, S. (1997) Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89, 495–498

    Article  PubMed  CAS  Google Scholar 

  11. Kushnirov, V. V. and Ter-Avanesyan, M. D. (1998) Structure and replication of yeast prions. Cell 94, 13–16

    Article  PubMed  CAS  Google Scholar 

  12. Liebman, S. W. and Derkatch, I. L. (1999) The yeast [PSI+] prion: making sense out of nonsense. J. Biol. Chem. 274, 1181–1184

    Article  PubMed  CAS  Google Scholar 

  13. Wickner, R. B. and Chernoff, Y. (1999) Prions of yeast and fungi: [URE3], [PSI] and [Het-s] discovered as heritable traits, in Prions (Prusiner, S. B. ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 229–272

    Google Scholar 

  14. Westaway, D., DeArmond, S. J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S.-L., et al. (1994) Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76, 117–129

    Article  PubMed  CAS  Google Scholar 

  15. Bueler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., Aguet, M., et al. (1993) Mice devoid of PrP are resistant to Scrapie. Cell 73, 1339–1347

    Article  PubMed  CAS  Google Scholar 

  16. Bueler, H., Fischer, M., Lang, Y., Bluethmann, H., Lipp, H. P., DeArmond, S. J., et al. 1992. Normal development and behavior of mice lacking the neuronal cellsurface PrP protein. Nature 356, 577–582

    Article  PubMed  CAS  Google Scholar 

  17. Cooper, T. G. (1982) Nitrogen metabolism in Saccharomyces cerevisiae, in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, vol. 2 (Strathern, J. N., Jones, E. W., and Broach, J. R. eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 39–99

    Google Scholar 

  18. Magasanik, B. (1992) Regulation of nitrogen utilization, in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, vol. 2 (Strathern, J. N., Jones, E. W., and Broach, J. R. eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 283–317

    Google Scholar 

  19. Chisholm, V. T., Lea, H. Z., Rai, R., and Cooper, T. G. (1987) Regulation of allantoate transport in wild-type and mutant strains of Saccharomyces cerevisiae. J. Bacteriol. 169, 1684–1690

    PubMed  CAS  Google Scholar 

  20. Rai, R., Genbauffe, F., Lea, H. Z., and Cooper, T. G. (1987) Transcriptional regulation of the DAL5 gene in Saccharomyces cerevisiae. J. Bacteriol. 169, 3521–3524

    PubMed  CAS  Google Scholar 

  21. Schoun, J. and Lacroute, F. (1969) Etude physiologique d’une mutation permettant l’incoporation d’acide ureidosuccinique chez la levure. C. R. Acad. Sci. 269, 1412–1414

    CAS  Google Scholar 

  22. Lacroute, F. (1971) Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106, 519–522

    PubMed  CAS  Google Scholar 

  23. Drillien, R. and Lacroute, F. (1972) Ureidosuccinic acid uptake in yeast and some aspects of its regulation. J. Bacteriol. 109, 203–208

    PubMed  CAS  Google Scholar 

  24. Drillien, R., Aigle, M., and Lacroute, F. (1973) Yeast mutants pleiotropically impaired in the regulation of the two glutamate dehydrogenases. Biochem. Biophys. Res. Commun. 53, 367–372

    Article  PubMed  CAS  Google Scholar 

  25. Aigle, M. and Lacroute, F. (1975) Genetical aspects of [URE3], a non-Mendelian, cytoplasmically inherited mutation in yeast. Mol. Gen. Genet. 136, 327–335

    Article  PubMed  CAS  Google Scholar 

  26. Mitchell, A. P. and Magasanik, B. (1984) Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae. Mol. Cell. Biol. 4, 2758–2766

    PubMed  CAS  Google Scholar 

  27. Courchesne, W. E. and Magasanik, B. (1988) Regulation of nitrogen assimilation in Saccharomyces cerevisiae: roles of the URE2 and GLN3 genes. J. Bacteriol. 170, 708–713

    PubMed  CAS  Google Scholar 

  28. Coschigano, P. W. and Magasanik, B. (1991) The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases. Mol. Cell. Biol. 11, 822–832

    PubMed  CAS  Google Scholar 

  29. Edskes, H. K., Hanover, J. A., and Wickner, R. B. (1999) Mks1p is a regulator of nitrogen catabolism upstream of Ure2p in Saccharomyces cerevisiae. Genetics 153, 585–594

    PubMed  CAS  Google Scholar 

  30. Beck, T. and Hall, M. N. (1999) The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Nature 402, 689–692

    Article  PubMed  CAS  Google Scholar 

  31. Cardenas, M. E., Cutler, N. S., Lorenz, M. C., Di Como, C. J., and Heitman, J. (1999) The TOR signaling cascade regulates gene expression in response to nutrients. Genes Dev. 13, 3271–3279

    Article  PubMed  CAS  Google Scholar 

  32. Hardwick, J. S., Kuruvilla, F. G., Tong, J. K., Shamji, A. F., and Schreiber, S. L. (1999) Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the tor proteins. Proc. Natl. Acad. Sci. USA 96, 14,866–14,870

    Article  PubMed  CAS  Google Scholar 

  33. Cox, B. S. (1965) PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 20, 505–521

    Article  Google Scholar 

  34. Young, C. S. H. and Cox, B. S. (1971) Extrachromosomal elements in a supersuppression system of yeast. 1. A nuclear gene controlling the inheritance of the extrachromosomal elements. Heredity 26, 413–422

    Article  Google Scholar 

  35. Young, C. S. H. and Cox, B. S. (1972) Extrachromosomal elements in a supersuppression system of yeast. II. Relations with other extrachromosomal elements. Heredity 28, 189–199

    Article  PubMed  CAS  Google Scholar 

  36. Leibowitz, M. J. and Wickner, R. B. (1978) Pet18: a chromosomal gene required for cell growth and for the maintenance of mitochondrial DNA and the killer plasmid of yeast. Mol. Gen. Genet. 165, 115–121

    Article  PubMed  CAS  Google Scholar 

  37. Cox, B. S., Tuite, M. F., and McLaughlin, C. S. (1988) The Psi factor of yeast: a problem in inheritance. Yeast 4, 159–179

    Article  PubMed  CAS  Google Scholar 

  38. Hawthorne, D. C. and Mortimer, R. K. (1968) Genetic mapping of nonsense suppressors in yeast. Genetics 60, 735–742

    PubMed  CAS  Google Scholar 

  39. Inge-Vechtomov, S. G. and Andrianova, V. M. (1970) Recessive super-suppressors in yeast. Genetika (Russ.) 6, 103–115

    Google Scholar 

  40. 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 SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365–4373

    PubMed  CAS  Google Scholar 

  41. Zhouravleva, G., Frolova, L., LeGoff, X., LeGuellec, R., Inge-Vectomov, S., Kisselev, L., et al. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065–4072

    PubMed  CAS  Google Scholar 

  42. Singh, A. C., Helms, C., and Sherman, F. (1979) Mutation of the non-Mendelian suppressor [PSI] in yeast by hypertonic media. Proc. Natl. Acad. Sci. USA 76, 1952–1956

    Article  PubMed  CAS  Google Scholar 

  43. Lund, P. M. and Cox, B. S. (1981) Reversion analysis of [psi-] mutations in Saccharomyces cerevisiae. Genet. Res. 37, 173–182

    Article  PubMed  CAS  Google Scholar 

  44. Chernoff, Y. O., Derkach, 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

    Article  PubMed  CAS  Google Scholar 

  45. 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

    PubMed  CAS  Google Scholar 

  46. TerAvanesyan, A., 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

    CAS  Google Scholar 

  47. Masison, D. C. and Wickner, R. B. (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270, 93–95

    Article  PubMed  CAS  Google Scholar 

  48. Masison, D. C., Maddelein, M.-L., and Wickner, R. B. (1997) The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc. Natl. Acad. Sci. USA 94, 12,503–12,508

    Article  PubMed  CAS  Google Scholar 

  49. Maddelein, M.-L. and Wickner, R. B. (1999) Two prion-inducing regions of Ure2p are non-overlapping. Mol. Cell. Biol. 19, 4516–4524

    PubMed  CAS  Google Scholar 

  50. TerAvanesyan, M. D., Kushnirov, V. V., Dagkesamanskaya, A. R., Didichenko, S. A., Chernoff, Y. O., Inge-Vechtomov, S. G., et al. (1993) Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683–692

    Article  CAS  Google Scholar 

  51. 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

    PubMed  CAS  Google Scholar 

  52. Kikuchi, Y., Shimatake, H., and Kikuchi, A. (1988) A yeast gene required for the G1 to S transition encodes a protein containing an A kinase target site and GTPase domain. EMBO J. 7, 1175–1182

    PubMed  CAS  Google Scholar 

  53. Kushnirov, V. V., TerAvanesyan, 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

    Article  PubMed  CAS  Google Scholar 

  54. Wilson, P. G. and Culbertson, M. R. (1988) SUF12 suppressor protein of yeast: a fusion protein related to the EF-1 family of elongation factors. J. Mol. Biol. 199, 559–573

    Article  PubMed  CAS  Google Scholar 

  55. Kochneva-Pervukhova, N. V., Poznyakovski, A. I., Smirnov, V. N., and Ter-Avanesyan, M. D. (1998) C-terminal truncation of the Sup35 protein increases the frequency of de novo gneration of a prion-based [PSI+] determinant in Saccharmyces cerevisiae. Curr. Genet. 34, 146–151

    Article  PubMed  CAS  Google Scholar 

  56. DePace, A. H., Santoso, A., Hillner, P., and Weissman, J. S. (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241–1252

    Article  PubMed  CAS  Google Scholar 

  57. Liu, J. J. and Lindquist, S. (1999) Oligopeptide-repeat expansions modulate protein-only’ inheritance in yeast. Nature 400, 573–576

    Article  PubMed  CAS  Google Scholar 

  58. Owen, F., Poulter, M., Lofthouse, R., Collinge, J., Crow, T. J., Risby, D. et al. (1989) Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet 1, 51–52

    Article  PubMed  CAS  Google Scholar 

  59. Fischer, M., Rulicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., et al. (1996) Prion protein (PrP) with amino-terminal deletions restoring susceptibility of PrPknockout mice to scrapie. EMBO J. 15, 1255–1264

    PubMed  CAS  Google Scholar 

  60. 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 SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127–3134

    PubMed  CAS  Google Scholar 

  61. 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

    Article  PubMed  CAS  Google Scholar 

  62. 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, 381–383

    Article  PubMed  CAS  Google Scholar 

  63. 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

    Article  PubMed  CAS  Google Scholar 

  64. Glover, J. R., Kowal, A. S., Shirmer, E. C., Patino, M. M., Liu, J.-J., and Lindquist, S. (1997) Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89, 811–819

    Article  PubMed  CAS  Google Scholar 

  65. Edskes, H. K., Gray, V. T., and Wickner, R. B. (1999) The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. USA 96, 1498–1503

    Article  PubMed  CAS  Google Scholar 

  66. Taylor, K. L., Cheng, N., Williams, R. W., Steven, A. C., and Wickner, R. B. (1999) Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283, 1339–1343

    Article  PubMed  CAS  Google Scholar 

  67. Chernoff, Y. O. and Ono, B.-I. (1992) Dosage-dependent modifiers of PSI-dependent omnipotent suppression in yeast, in Protein Synthesis and Targeting in Yeast, (Brown, A. J. P., Tuite, M. F., and McCarthy J. E. G., eds.), Springer-Verlag, Berlin. pp. 101–107

    Google Scholar 

  68. Chernoff, Y. O., Lindquist, S. L., Ono, B.-I., Inge-Vechtomov, S. G., and Liebman, S. W. (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268, 880–884

    Article  PubMed  CAS  Google Scholar 

  69. Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475–478

    Article  PubMed  CAS  Google Scholar 

  70. Sanchez, V. and Lindquist, S. L. (1990) HSP104 required for induced thermotolerance. Science 248, 1112–1115

    Article  PubMed  CAS  Google Scholar 

  71. James, P., Pfund, C., and Craig, E. A. (1997) Functional specificity among Hsp70 molecular chaperones. Science 275, 387–389

    Article  PubMed  CAS  Google Scholar 

  72. Ziegelhoffer, T., Johnson, J. L., and Craig, E. A. (1996) Chaperones get Hip. protein folding. Curr Biol. 6, 272–275

    Article  PubMed  CAS  Google Scholar 

  73. Newnam, G. P., Wegrzyn, R. D., Lindquist, S. L., and Chernoff, Y. O. (1999) Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19, 1325–1333

    PubMed  CAS  Google Scholar 

  74. Pfund, C., Lopez-Hoyo, N., Ziegelhoffer, T., Schilke, B. A., Lopez-Buesa, P., Walter, W. A., et al. (1998) The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17, 3981–3989

    Article  PubMed  CAS  Google Scholar 

  75. Chernoff, Y. O., Newnam, G. P., Kumar, J., Allen, K., and Zink, A. D. (1999) Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability and toxicity of the [PSI+] prion. Mol. Cell. Biol. 19, 8103–8112

    PubMed  CAS  Google Scholar 

  76. Matsuura, A. and Anraku, Y. (1993) Characterization of the MKS1 gene, a new negative regulator of the ras-cyclic AMP pathway in Saccharomyces cerevisiae. Mol. Gen. Genet. 238, 6–16

    PubMed  CAS  Google Scholar 

  77. Feller, A., Ramos, F., Peirard, A., and Dubois, E. (1997) Lys80p of Saccharomyces cerevisiae, previously proposed as a specific repressor of LYS genes, is a pleiotropic regulatory factor identical to Mks1p. Yeast 13, 1337–1346

    Article  PubMed  CAS  Google Scholar 

  78. Derkatch, I. L., Bradley, M. E., and Liebman, S. W. (1998) Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion. Proc Natl Acad Sci USA 95, 2400–2405

    Article  PubMed  CAS  Google Scholar 

  79. Derkatch, I. L., Bradley, M. E., Zhou, P., Chernoff, Y. O., and Liebman, S. W. (1997) Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147, 507–519.

    PubMed  CAS  Google Scholar 

  80. Begueret, J., Turq, B., and Clave, C. (1994) Vegetative incompatibility in filamentous fungi: het genes begin to talk. Trends Genet. 10, 441–446.

    Article  PubMed  CAS  Google Scholar 

  81. Rizet, G. (1952) Les phenomenes de barrage chez Podospora anserina: analyse genetique des barrages entre les souches s et S. Rev. Cytol. Biol. Veg. 13, 51–92.

    Google Scholar 

  82. Beisson-Schecroun, J. (1962) Incompatibilte cellulaire et interactions nucleocytoplasmiques dans les phenomenes de barrage chez Podospora anserina. Ann. Genet. 4, 3–50.

    Google Scholar 

  83. Coustou, V., Deleu, C., Saupe, S. J., and Begueret, J. (1999) Mutational analysis of the [Het-s] prion analog of Podospora anserina: a short N-terminal peptide allows prion propagation. Genetics 153, 1629–1640.

    PubMed  CAS  Google Scholar 

  84. Tuite, M. F., Mundy, C. R., and Cox, B. S. (1981) Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 98, 691–711.

    PubMed  CAS  Google Scholar 

  85. Eaglestone, S. S., Ruddock, L. W., Cox, B. S., and Tuite, M. F. (2000) Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97, 240–244.

    Article  PubMed  CAS  Google Scholar 

  86. Bousset, L., Beirhali, H., Janin, J., Melki, R., and Morera, S. (2001) Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae Structure 9, 39–46.

    CAS  Google Scholar 

  87. Chernoff, Y. O., Galkin, A. P., Lewitin, E., Chernova, T. A., Newnam, G. P., and Belenkly, S. M. (2000). Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein. Molec. Microbiol. 35, 865–876.

    Article  CAS  Google Scholar 

  88. Choi, J. H., Lou, W., and Vancura, A. (1998) A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273, 29,915–19,922.

    Article  PubMed  CAS  Google Scholar 

  89. Jung, G., Jones, G., Wegrzyn, R. D., and Masison, D. C. (2000) A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress. Genetics 156, 559–570.

    PubMed  CAS  Google Scholar 

  90. Jung, G., and Masison, D. C. (2001) Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol. Submitted.

    Google Scholar 

  91. Kushnirov, V. V., Kochneva-Pervukhova, N. V., Cechenova, M. B., Frolova, N. S., and Ter-Avanesyan, M. D. (2000) Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J. 19, 324–331.

    Article  PubMed  CAS  Google Scholar 

  92. Kushnirov, V. V., Ter-Avanesyan, M. D., Didichenko, S. A., Smirnov, V. N., Chernoff, Y. O., Derkach, I. L. et al. (1990) Divergence and conservation of SUP2 (SUP35) gene of yeasts Pichia pinus and Saccharomyces cerevisiae. Yeast 6, 461–472.

    Article  PubMed  CAS  Google Scholar 

  93. Moriyama, H., Edskes, H. K., and Wickner, R. B. (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20, 8916–8922.

    Article  PubMed  CAS  Google Scholar 

  94. Santoso, A., Chien, P. Osherovich, L. Z., and Weissman, J. S. (2000) Molecular basis of a yeast prion species barrier. Cell 100, 277–288.

    Article  PubMed  CAS  Google Scholar 

  95. Sondheimer, N. and Lindquist, S. (2000) Rnq1: An epigenetic modifier of preotein function inyeast. Molec. Cell 5, 163–172.

    Article  PubMed  CAS  Google Scholar 

  96. Speransky, V. Taylor, K. L. Edskes, H. K. Wickner, R. B., and Steven, A., (2001). Prion filament networks in [URE3] cells of Saccharomyces cerevisiae. J. Cell. Biol. submitted.

    Google Scholar 

  97. Umland, T. C., Taylor, K. L. Rhee, S., Wickner, R. B., and Davies, D. R. (2001). The crystal structure of the nitrogen catabolite regulatory fragment of the yeast prion protein Ure2p. Proc. natl. Acad. Sci. USA 98, 1459–1464.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD

    Reed B. Wickner, Herman K. Edskes, Kimberly L. Taylor, Marie-Lise Maddelein, Hiromitsu Moriyama & B. Tibor Roberts

Authors
  1. Reed B. Wickner
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Herman K. Edskes
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Kimberly L. Taylor
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Marie-Lise Maddelein
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Hiromitsu Moriyama
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. B. Tibor Roberts
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Department of Experimental Psychology, MRC Comparative Cognition Team, School of Clinical Veterinary Medicine, Cambridge, UK

    Harry F. Baker

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Humana Press Inc.

About this protocol

Cite this protocol

Wickner, R.B., Edskes, H.K., Taylor, K.L., Maddelein, ML., Moriyama, H., Tibor Roberts, B. (2001). Prions of Yeast From Cytoplasmic Genes to Heritable Amyloidosis. In: Baker, H.F. (eds) Molecular Pathology of the Prions. Methods in Molecular Medicine™, vol 59. Humana Press. https://doi.org/10.1385/1-59259-134-5:237

Download citation

  • DOI: https://doi.org/10.1385/1-59259-134-5:237

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-924-7

  • Online ISBN: 978-1-59259-134-3

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics

Search

Navigation