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Science 22 April 1994:
Vol. 264. no. 5158, pp. 566 - 569
DOI: 10.1126/science.7909170
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Articles

Science, Vol 264, Issue 5158, 566-569
Copyright © 1994 by American Association for the Advancement of Science

articles

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

RB Wickner

Section on Genetics of Simple Eukaryotes, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

A cytoplasmically inherited element, [URE3], allows yeast to use ureidosuccinate in the presence of ammonium ion. Chromosomal mutations in the URE2 gene produce the same phenotype. [URE3] depends for its propagation on the URE2 product (Ure2p), a negative regulator of enzymes of nitrogen metabolism. Saccharomyces cerevisiae strains cured of [URE3] with guanidium chloride were shown to return to the [URE3]-carrying state without its introduction from other cells. Overproduction of Ure2p increased the frequency with which a strain became [URE3] by 100-fold. In analogy to mammalian prions, [URE3] may be an altered form of Ure2p that is inactive for its normal function but can convert normal Ure2p to the altered form. The genetic evidence presented here suggests that protein-based inheritance, involving a protein unrelated to the mammalian prion protein, can occur in a microorganism.


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Yeast prions [URE3] and [PSI+] are diseases.
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Strain-specific morphologies of yeast prion amyloid fibrils.
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J. Biol. Chem. 280, 13220-13228
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Hsp70 Chaperones as Modulators of Prion Life Cycle: Novel Effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+].
K. D. Allen, R. D. Wegrzyn, T. A. Chernova, S. Muller, G. P. Newnam, P. A. Winslett, K. B. Wittich, K. D. Wilkinson, and Y. O. Chernoff (2005)
Genetics 169, 1227-1242
   Abstract »    Full Text »    PDF »
Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication.
Y. Song, Y.-x. Wu, G. Jung, Y. Tutar, E. Eisenberg, L. E. Greene, and D. C. Masison (2005)
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   Abstract »    Full Text »    PDF »
Notch-1 activation and dendritic atrophy in prion disease.
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PNAS 102, 886-891
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Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It.
Y. Inoue, H. Taguchi, A. Kishimoto, and M. Yoshida (2004)
J. Biol. Chem. 279, 52319-52323
   Abstract »    Full Text »    PDF »
The [URE3] Yeast Prion Results from Protein Aggregates That Differ from Amyloid Filaments Formed in Vitro.
L. Ripaud, L. Maillet, F. Immel-Torterotot, F. Durand, and C. Cullin (2004)
J. Biol. Chem. 279, 50962-50968
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Specificity of Prion Assembly in Vivo: [PSI+] AND [PIN+] FORM SEPARATE STRUCTURES IN YEAST.
S. Bagriantsev and S. W. Liebman (2004)
J. Biol. Chem. 279, 51042-51048
   Abstract »    Full Text »    PDF »
The Yeast Prion Protein Ure2 Shows Glutathione Peroxidase Activity in Both Native and Fibrillar Forms.
M. Bai, J.-M. Zhou, and S. Perrett (2004)
J. Biol. Chem. 279, 50025-50030
   Abstract »    Full Text »    PDF »
Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.
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PNAS 101, 12934-12939
   Abstract »    Full Text »    PDF »
Scrambled Prion Domains Form Prions and Amyloid.
E. D. Ross, U. Baxa, and R. B. Wickner (2004)
Mol. Cell. Biol. 24, 7206-7213
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The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions.
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Synthetic Mammalian Prions.
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A model for Ure2p prion filaments and other amyloids: The parallel superpleated {beta}-structure.
A. V. Kajava, U. Baxa, R. B. Wickner, and A. C. Steven (2004)
PNAS 101, 7885-7890
   Abstract »    Full Text »    PDF »
Propagation of Saccharomyces cerevisiae [PSI+] Prion Is Impaired by Factors That Regulate Hsp70 Substrate Binding.
G. Jones, Y. Song, S. Chung, and D. C. Masison (2004)
Mol. Cell. Biol. 24, 3928-3937
   Abstract »    Full Text »    PDF »
Prions: proteins as genes and infectious entities.
R. B. Wickner, H. K. Edskes, B. T. Roberts, U. Baxa, M. M. Pierce, E. D. Ross, and A. Brachmann (2004)
Genes & Dev. 18, 470-485
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S. Kicka and P. Silar (2004)
Genetics 166, 1241-1252
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J. Biol. Chem. 279, 7378-7383
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I. V. Baskakov (2004)
J. Biol. Chem. 279, 7671-7677
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A non-chromosomal factor allows viability of Schizosaccharomyces pombe lacking the essential chaperone calnexin.
P. Collin, P. B. Beauregard, A. Elagoz, and L. A. Rokeach (2004)
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Amyloid Nucleation and Hierarchical Assembly of Ure2p Fibrils: ROLE OF ASPARAGINE/GLUTAMINE REPEAT AND NONREPEAT REGIONS OF THE PRION DOMAIN.
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Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104.
D. S. Kryndushkin, I. M. Alexandrov, M. D. Ter-Avanesyan, and V. V. Kushnirov (2003)
J. Biol. Chem. 278, 49636-49643
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Genetics 165, 1675-1685
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J. Biol. Chem. 278, 43717-43727
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Analysis of the Generation and Segregation of Propagons: Entities That Propagate the [PSI+] Prion in Yeast.
B. Cox, F. Ness, and M. Tuite (2003)
Genetics 165, 23-33
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Heritable activity: a prion that propagates by covalent autoactivation.
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Genes & Dev. 17, 2083-2087
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Assembly of the Yeast Prion Ure2p into Protein Fibrils: THERMODYNAMIC AND KINETIC CHARACTERIZATION.
N. Fay, Y. Inoue, L. Bousset, H. Taguchi, and R. Melki (2003)
J. Biol. Chem. 278, 30199-30205
   Abstract »    Full Text »    PDF »
Conservation of the Prion Properties of Ure2p through Evolution.
A. Baudin-Baillieu, E. Fernandez-Bellot, F. Reine, E. Coissac, and C. Cullin (2003)
Mol. Biol. Cell 14, 3449-3458
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Atypical Effect of Salts on the Thermodynamic Stability of Human Prion Protein.
A. C. Apetri and W. K. Surewicz (2003)
J. Biol. Chem. 278, 22187-22192
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Ure2, a Prion Precursor with Homology to Glutathione S-Transferase, Protects Saccharomyces cerevisiae Cells from Heavy Metal Ion and Oxidant Toxicity.
R. Rai, J. J. Tate, and T. G. Cooper (2003)
J. Biol. Chem. 278, 12826-12833
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Karyopherin-Mediated Nuclear Import of the Homing Endonuclease VMA1-Derived Endonuclease Is Required for Self-Propagation of the Coding Region.
Y. Nagai, S. Nogami, F. Kumagai-Sano, and Y. Ohya (2003)
Mol. Cell. Biol. 23, 1726-1736
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Saccharomyces cerevisiae Hsp70 Mutations Affect [PSI+] Prion Propagation and Cell Growth Differently and Implicate Hsp40 and Tetratricopeptide Repeat Cochaperones in Impairment of [PSI+].
G. W. Jones and D. C. Masison (2003)
Genetics 163, 495-506
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Disease-associated F198S Mutation Increases the Propensity of the Recombinant Prion Protein for Conformational Conversion to Scrapie-like Form.
D. L. Vanik and W. K. Surewicz (2002)
J. Biol. Chem. 277, 49065-49070
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Guanidine Hydrochloride Inhibits the Generation of Prion "Seeds" but Not Prion Protein Aggregation in Yeast.
F. Ness, P. Ferreira, B. S. Cox, and M. F. Tuite (2002)
Mol. Cell. Biol. 22, 5593-5605
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A Heritable Structural Alteration of the Yeast Mitochondrion.
D. Lockshon (2002)
Genetics 161, 1425-1435
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Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.
G. Jung, G. Jones, and D. C. Masison (2002)
PNAS 99, 9936-9941
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Progress toward an ultimate proof of the prion hypothesis.
S. W. Liebman (2002)
PNAS 99, 9098-9100
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A Gene from Aspergillus nidulans with Similarity to URE2 of Saccharomyces cerevisiae Encodes a Glutathione S-Transferase Which Contributes to Heavy Metal and Xenobiotic Resistance.
J. A. Fraser, M. A. Davis, and M. J. Hynes (2002)
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Antagonistic Interactions between Yeast [PSI+] and [URE3] Prions and Curing of [URE3] by Hsp70 Protein Chaperone Ssa1p but Not by Ssa2p.
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B. Cosson, A. Couturier, S. Chabelskaya, D. Kiktev, S. Inge-Vechtomov, M. Philippe, and G. Zhouravleva (2002)
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   Abstract »    Full Text »    PDF »
Inaugural Article: Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.
U. Baxa, V. Speransky, A. C. Steven, and R. B. Wickner (2002)
PNAS 99, 5253-5260
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Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta -peptide of amyloid plaques.
M. F. Perutz, B. J. Pope, D. Owen, E. E. Wanker, and E. Scherzinger (2002)
PNAS 99, 5596-5600
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The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism.
C. Resende, S. N. Parham, C. Tinsley, P. Ferreira, J. A. B. Duarte, and M. F. Tuite (2002)
Microbiology 148, 1049-1060
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Convergence of TOR-Nitrogen and Snf1-Glucose Signaling Pathways onto Gln3.
P. G. Bertram, J. H. Choi, J. Carvalho, T.-F. Chan, W. Ai, and X. F. S. Zheng (2002)
Mol. Cell. Biol. 22, 1246-1252
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Novel Non-Mendelian Determinant Involved in the Control of Translation Accuracy in Saccharomyces cerevisiae.
K. V. Volkov, A. Yu. Aksenova, M. J. Soom, K. V. Osipov, A. V. Svitin, C. Kurischko, I. S. Shkundina, M. D. Ter-Avanesyan, S. G. Inge-Vechtomov, and L. N. Mironova (2002)
Genetics 160, 25-36
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Induction of Distinct [URE3] Yeast Prion Strains.
M. Schlumpberger, S. B. Prusiner, and I. Herskowitz (2001)
Mol. Cell. Biol. 21, 7035-7046
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Molecular Population Genetics and Evolution of a Prion-like Protein in Saccharomyces cerevisiae.
M. A. Jensen, H. L. True, Y. O. Chernoff, and S. Lindquist (2001)
Genetics 159, 527-535
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