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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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J. Biol. Chem. 279, 52319-52323
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   Abstract »    Full Text »    PDF »
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 »
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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
   Abstract »    Full Text »    PDF »
The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions.
Y. Kimura, S. Koitabashi, A. Kakizuka, and T. Fujita (2004)
Genes Cells 9, 685-696
   Abstract »    Full Text »    PDF »
Synthetic Mammalian Prions.
G. Legname, I. V. Baskakov, H.-O. B. Nguyen, D. Riesner, F. E. Cohen, S. J. DeArmond, and S. B. Prusiner (2004)
Science 305, 673-676
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A. V. Kajava, U. Baxa, R. B. Wickner, and A. C. Steven (2004)
PNAS 101, 7885-7890
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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
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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)
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S. Kicka and P. Silar (2004)
Genetics 166, 1241-1252
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The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104.
V. Grimminger, K. Richter, A. Imhof, J. Buchner, and S. Walter (2004)
J. Biol. Chem. 279, 7378-7383
   Abstract »    Full Text »    PDF »
Autocatalytic Conversion of Recombinant Prion Proteins Displays a Species Barrier.
I. V. Baskakov (2004)
J. Biol. Chem. 279, 7671-7677
   Abstract »    Full Text »    PDF »
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)
J. Cell Sci. 117, 907-918
   Abstract »    Full Text »    PDF »
Amyloid Nucleation and Hierarchical Assembly of Ure2p Fibrils: ROLE OF ASPARAGINE/GLUTAMINE REPEAT AND NONREPEAT REGIONS OF THE PRION DOMAIN.
Y. Jiang, H. Li, L. Zhu, J.-M. Zhou, and S. Perrett (2004)
J. Biol. Chem. 279, 3361-3369
   Abstract »    Full Text »    PDF »
Prions of Yeast Are Genes Made of Protein: Amyloids and Enzymes.
R.B. WICKNER, H.K. EDSKES, E.D. ROSS, M.M. PIERCE, F. SHEWMAKER, U. BAXA, and A. BRACHMANN (2004)
Cold Spring Harb Symp Quant Biol 69, 489-496
   Abstract »    PDF »
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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Destabilizing Interactions Among [PSI+] and [PIN+] Yeast Prion Variants.
M. E. Bradley and S. W. Liebman (2003)
Genetics 165, 1675-1685
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Architecture of Ure2p Prion Filaments: THE N-TERMINAL DOMAINS FORM A CENTRAL CORE FIBER.
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Conservation of the Prion Properties of Ure2p through Evolution.
A. Baudin-Baillieu, E. Fernandez-Bellot, F. Reine, E. Coissac, and C. Cullin (2003)
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R. Rai, J. J. Tate, and T. G. Cooper (2003)
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Y. Nagai, S. Nogami, F. Kumagai-Sano, and Y. Ohya (2003)
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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.
C. Schwimmer and D. C. Masison (2002)
Mol. Cell. Biol. 22, 3590-3598
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Amyloid aggregates of the HET-s prion protein are infectious.
M.-L. Maddelein, S. Dos Reis, S. Duvezin-Caubet, B. Coulary-Salin, and S. J. Saupe (2002)
PNAS 99, 7402-7407
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Poly(A)-Binding Protein Acts in Translation Termination via Eukaryotic Release Factor 3 Interaction and Does Not Influence [PSI+] Propagation.
B. Cosson, A. Couturier, S. Chabelskaya, D. Kiktev, S. Inge-Vechtomov, M. Philippe, and G. Zhouravleva (2002)
Mol. Cell. Biol. 22, 3301-3315
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P. G. Bertram, J. H. Choi, J. Carvalho, T.-F. Chan, W. Ai, and X. F. S. Zheng (2002)
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   Abstract »    Full Text »    PDF »
Novel Non-Mendelian Determinant Involved in the Control of Translation Accuracy in Saccharomyces cerevisiae.
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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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Mechanism of Prion Loss after Hsp104 Inactivation in Yeast.
R. D. Wegrzyn, K. Bapat, G. P. Newnam, A. D. Zink, and Y. O. Chernoff (2001)
Mol. Cell. Biol. 21, 4656-4669
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Prion Filament Networks in [URE3] Cells of Saccharomyces cerevisiae.
V. V. Speransky, K. L. Taylor, H. K. Edskes, R. B. Wickner, and A. C. Steven (2001)
J. Cell Biol. 153, 1327-1336
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Endless possibilities: translation termination and stop codon recognition.
G. Bertram, S. Innes, O. Minella, J. P. Richardson, and I. Stansfield (2001)
Microbiology 147, 255-269
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Multigenerational Cortical Inheritance of the Rax2 Protein in Orienting Polarity and Division in Yeast.
T. Chen, T. Hiroko, A. Chaudhuri, F. Inose, M. Lord, S. Tanaka, J. Chant, and A. Fujita (2000)
Science 290, 1975-1978
   Abstract »    Full Text »
The Level of DAL80 Expression Down-Regulates GATA Factor-Mediated Transcription in Saccharomyces cerevisiae.
T. S. Cunningham, R. Rai, and T. G. Cooper (2000)
J. Bacteriol. 182, 6584-6591
   Abstract »    Full Text »


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