Antagonistic Interactions between Yeast [PSI⁺] and [URE3] Prions and Curing of [URE3] by Hsp70 Protein Chaperone Ssa1p but Not by Ssa2p

REFERENCES

• Chernoff, Y. O., I. L. Derkatch, and S. G. Inge-Vechtomov. 1993. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24: 268–270.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O., S. L. Lindquist, B. Ono, S. G. Inge-Vechtomov, and S. W. Liebman. 1995. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268: 880–884.
   PubMed Web of Science ®Google Scholar
• Cox, K. H., R. Rai, M. Distler, J. R. Daugherty, J. A. Coffman, and T. G. Cooper. 2000. Saccharomyces cerevisiae GATA sequences function as TATA elements during nitrogen catabolite repression and when Gln3p is excluded from the nucleus by overproduction of Ure2p. J. Biol. Chem. 275: 17611–17618.
   PubMed Web of Science ®Google Scholar
• DebBurman, S. K., G. J. Raymond, B. Caughey, and S. Lindquist. 1997. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA 94: 13938–13943.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., M. E. Bradley, J. Y. Hong, and S. W. Liebman. 2001. Prions affect the appearance of other prions. The story of [PIN+]. Cell 106: 171–182.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., M. E. Bradley, P. Zhou, Y. O. Chernoff, and S. W. Liebman. 1997. Genetic and environmental factors affecting the de-novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147: 509–519.
   Google Scholar
• Doel, S. M., S. J. McCready, C. R. Nierras, and B. S. Cox. 1994. The dominant PNM2 − mutation which eliminates the Ψ factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137: 659–670.
   PubMed Web of Science ®Google Scholar
• Edskes, H. K., V. T. Gray, and R. B. Wickner. 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.
   PubMed Web of Science ®Google Scholar
• Edskes, H. K., and R. B. Wickner. 2000. A protein required for prion generation: [URE3] induction requires the Ras-regulated Mks1 protein. Proc. Natl. Acad. Sci. USA 97: 6625–6629.
   PubMedGoogle Scholar
• Ellwood, M. S., and E. A. Craig. 1984. Differential regulation of the 70K heat shock gene and related genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 4: 1454–1459.
   PubMedGoogle Scholar
• Fernandez-Bellot, E., E. Guillemet, F. Ness, A. Baudin-Baillieu, L. Ripaud, M. Tuite, and C. Cullin. 2002. The [URE3] phenotype: evidence for a soluble prion in yeast. EMBO Rep. 3: 76–81.
   PubMedGoogle Scholar
• Glover, J. R., A. S. Kowal, E. C. Schirmer, M. M. Patino, J.-J. Liu, and S. Lindquist. 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89: 811–819.
   PubMed Web of Science ®Google Scholar
• Jung, G., G. Jones, R. D. Wegrzyn, and D. C. Masison. 2000. A role for cytosolic Hsp70 in yeast [PSI +] prion propagation and [PSI +] as a cellular stress. Genetics 156: 559–570.
   PubMed Web of Science ®Google Scholar
• King, C. Y., P. Tittmann, H. Gross, R. Gebert, M. Aebi, and K. Wuthrich. 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.
   PubMed Web of Science ®Google Scholar
• Kochneva-Pervukhova, N. V., S. V. Paushkin, V. V. Kushnirov, B. S. Cox, M. F. Tuite, and M. D. Ter-Avanesyan. 1998. Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein. EMBO J. 17: 5805–5810.
   PubMed Web of Science ®Google Scholar
• Kushnirov, V. V., and M. D. Ter-Avanesyan. 1998. Structure and replication of yeast prions. Cell 94: 13–16.
   PubMed Web of Science ®Google Scholar
• Lacroute, F. 1971. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106: 519–522.
   PubMed Web of Science ®Google Scholar
• Lansbury, P. T., Jr., and B. Caughey. 1995. The chemistry of scrapie infection: implications of the ′ice 9′ metaphor. Chem. Biol. 2: 1–5.
   PubMed Web of Science ®Google Scholar
• Lindquist, S., and G. Kim. 1996. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. USA 93: 5301–5306.
   PubMed Web of Science ®Google Scholar
• Masison, D. C., M.-L. Maddelein, and R. B. Wickner. 1997. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc. Natl. Acad. Sci. USA 94: 12503–12508.
   PubMed Web of Science ®Google Scholar
• Masison, D. C., and R. B. Wickner. 1995. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 273: 93–95.
   Google Scholar
• Miller, J. F. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Moriyama, H., H. K. Edskes, and R. B. Wickner. 2000. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20: 8916–8922.
   PubMed Web of Science ®Google Scholar
• Newnam, G. P., R. D. Wegrzyn, S. L. Lindquist, and Y. O. Chernoff. 1999. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19: 1325–1333.
   PubMed Web of Science ®Google Scholar
• Osherovich, L. Z., and J. S. Weissman. 2001. Multiple gln/asn-rich prion domains confer susceptibility to induction of the yeast. Cell 106: 183–194.
   PubMed Web of Science ®Google Scholar
• Parsell, D. A., A. S. Kowal, M. A. Singer, and S. Lindquist. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372: 475–478.
   PubMed Web of Science ®Google Scholar
• Patino, M. M., J.-J. Liu, J. R. Glover, and S. Lindquist. 1996. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273: 622–626.
   PubMed Web of Science ®Google Scholar
• Paushkin, S. V., V. V. Kushnirov, V. N. Smirnov, and M. D. Ter-Avanesyan. 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 Web of Science ®Google Scholar
• Priola, S. A., B. Caughey, R. E. Race, and B. Chesebro. 1994. Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. J. Virol. 68: 4873–4878.
   PubMed Web of Science ®Google Scholar
• Prusiner, S. B., M. Scott, D. Foster, K. M. Pan, D. Groth, C. Mirenda, M. Torchia, S. L. Yang, D. Serban, G. A. Carlson, et al. 1990. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673–686.
   PubMed Web of Science ®Google Scholar
• Rai, R., F. S. Genbauffe, R. A. Sumrada, and T. G. Cooper. 1989. Identification of sequences responsible for transcriptional activation of the allantoate permease gene in Saccharomyces cerevisiae. Mol. Cell. Biol. 9: 602–608.
   PubMedGoogle Scholar
• Serio, T. R., A. G. Cashikar, A. S. Kowal, G. J. Sawicki, J. J. Moslehi, L. Serpell, M. F. Arnsdorf, and S. L. Lindquist. 2000. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317–1321.
   PubMed Web of Science ®Google Scholar
• Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19–27.
   PubMed Web of Science ®Google Scholar
• Sondheimer, N., N. Lopez, E. A. Craig, and S. Lindquist. 2001. The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J. 20: 2435–2442.
   PubMed Web of Science ®Google Scholar
• Stansfield, I., K. M. Jones, V. V. Kushnirov, A. R. Dagkesamanskaya, A. I. Poznyakovski, S. V. Paushkin, C. R. Nierras, B. S. Cox, M. D. Ter-Avanesyan, and M. F. Tuite. 1995. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14: 4365–4373.
   PubMed Web of Science ®Google Scholar
• Stone, D. E., and E. A. Craig. 1990. Self-regulation of 70-kilodalton heat shock proteins in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 1622–1632.
   PubMed Web of Science ®Google Scholar
• Taylor, K. L., N. Cheng, R. W. Williams, A. C. Steven, and R. B. Wickner. 1999. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283: 1339–1343.
   PubMed Web of Science ®Google Scholar
• Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10: 1793–1808.
   PubMed Web of Science ®Google Scholar
• Wickner, R. B. 1994. Evidence for a prion analog in S. cerevisiae: the [URE3] non-Mendelian genetic element as an altered URE2 protein. Science 264: 566–569.
   PubMed Web of Science ®Google Scholar