The yeast prion protein Ure2: Structure, function and folding

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 3, 2006, Pages 535-545

  Lian, Hui Yong ^a,b   Jiang, Yi ^a   Zhang, Hong ^a,b   Jones, Gary W ^c   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c NATIONAL UNIVERSITY OF IRELAND   (Ireland)

Author keywords

Amyloid; Chaperone; Glutathione transferase; Peroxidase; Prion; Protein Folding

Indexed keywords

AMYLOID; CHAPERONE; ENZYME; FUNGAL PROTEIN; GLUTATHIONE; GLUTATHIONE TRANSFERASE; NITROGEN; PEROXIDASE; PRION PROTEIN; PROTEIN URE2; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; ENZYME ACTIVITY; GENE MUTATION; INTERMETHOD COMPARISON; NITROGEN METABOLISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; SACCHAROMYCES CEREVISIAE; YEAST;

AMINO ACID SEQUENCE; MOLECULAR SEQUENCE DATA; PRIONS; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION;

SACCHAROMYCES CEREVISIAE;

EID: 33645993282     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.11.016     Document Type: Review

References (120)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13363-13383
2. Hope J., Reekie L.J., Hunter N., Multhaup G., Beyreuther K., White H., Scott A.C., Stack M.J., Dawson M., and Wells G.A. Fibrils from brains of cows with new cattle disease contain scrapie-associated protein. Nature 336 (1988) 390-392
3. Will R.G., Ironside J.W., Zeidler M., Cousens S.N., Estibeiro K., Alperovitch A., Poser S., Pocchiari M., Hofman A., and Smith P.G. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347 (1996) 921-925
4. Legname G., Baskakov I.V., Nguyen H.O., Riesner D., Cohen F.E., DeArmond S.J., and Prusiner S.B. Synthetic mammalian prions. Science 305 (2004) 673-676
5. Castilla J., Saa P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
6. Zou W.Q., and Gambetti P. From microbes to prions the final proof of the prion hypothesis. Cell 121 (2005) 155-157
7. Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264 (1994) 566-569
8. Wickner R.B., Edskes H.K., Ross E.D., Pierce M.M., Baxa U., Brachmann A., and Shewmaker F. Prion genetics: new rules for a new kind of gene. Annu. Rev. Genet. 38 (2004) 681-707
9. Shorter J., and Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat. Rev., Genet. 6 (2005) 435-450
10. Cox B.S. A cytoplasmic suppressor of super-suppressor in yeast. Heredity 20 (1965) 205-221
11. Chernoff Y.O., Derkach I.L., and Inge-Vechtomov S.G. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24 (1993) 268-270
12. Patino M.M., Liu J.J., Glover J.R., and Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273 (1996) 622-626
13. Sondheimer N., and Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 5 (2000) 163-172
14. Derkatch I.L., Bradley M.E., Hong J.Y., and Liebman S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106 (2001) 171-182
15. Michelitsch M.D., and Weissman J.S. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 11910-11915
16. Coustou V., Deleu C., Saupe S., and Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 9773-9778
17. Dos R.S., Coulary-Salin B., Forge V., Lascu I., Begueret J., and Saupe S.J. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J. Biol. Chem. 277 (2002) 5703-5706
18. Maddelein M.L., Dos R.S., Duvezin-Caubet S., Coulary-Salin B., and Saupe S.J. Amyloid aggregates of the HET-s prion protein are infectious. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 7402-7407
19. King C.Y., and Az-Avalos R. Protein-only transmission of three yeast prion strains. Nature 428 (2004) 319-323
20. Tanaka M., Chien P., Naber N., Cooke R., and Weissman J.S. Conformational variations in an infectious protein determine prion strain differences. Nature 428 (2004) 323-328
21. Brachmann A., Baxa U., and Wickner R.B. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J. 24 (2005) 3082-3092
22. Balguerie A., Dos R.S., Ritter C., Chaignepain S., Coulary-Salin B., Forge V., Bathany K., Lascu I., Schmitter J.M., Riek R., and Saupe S.J. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J. 22 (2003) 2071-2081
23. James T.L., Liu H., Ulyanov N.B., Farr-Jones S., Zhang H., Donne D.G., Kaneko K., Groth D., Mehlhorn I., Prusiner S.B., and Cohen F.E. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 10086-10091
24. Zahn R., Liu A., Luhrs T., Riek R., von S.C., Lopez G.F., Billeter M., Calzolai L., Wider G., and Wuthrich K. NMR solution structure of the human prion protein. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 145-150
25. Hornshaw M.P., McDermott J.R., and Candy J.M. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207 (1995) 621-629
26. Thual C., Komar A.A., Bousset L., Fernandez-Bellot E., Cullin C., and Melki R. Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J. Biol. Chem. 274 (1999) 13666-13674
27. Perrett S., Freeman S.J., Butler P.J., and Fersht A.R. Equilibrium folding properties of the yeast prion protein determinant Ure2. J. Mol. Biol. 290 (1999) 331-345
28. Umland T.C., Taylor K.L., Rhee S., Wickner R.B., and Davies D.R. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 1459-1464
29. Coschigano P.W., and Magasanik B. 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 (1991) 822-832
30. Cooper T.G. Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to the GATA factors: connecting the dots. FEMS Microbiol. Rev. 26 (2002) 223-238
31. Masison D.C., and Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270 (1995) 93-95
32. Taylor K.L., Cheng N., Williams R.W., Steven A.C., and Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283 (1999) 1339-1343
33. Thual C., Bousset L., Komar A.A., Walter S., Buchner J., Cullin C., and Melki R. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry 40 (2001) 1764-1773
34. Jiang Y., Li H., Zhu L., Zhou J.M., and Perrett S. Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domain. J. Biol. Chem. 279 (2004) 3361-3369
35. Galani D., Fersht A.R., and Perrett S. Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates. J. Mol. Biol. 315 (2002) 213-227
36. Zhu L., Zhang X.J., Wang L.Y., Zhou J.M., and Perrett S. Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. J. Mol. Biol. 328 (2003) 235-254
37. Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24 (1999) 58-63
38. Perutz M.F., Johnson T., Suzuki M., and Finch J.T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 5355-5358
39. Perutz M.F., Pope B.J., Owen D., Wanker E.E., and Scherzinger E. 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. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 5596-5600
40. Thakur A.K., and Wetzel R. Mutational analysis of the structural organization of polyglutamine aggregates. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 17014-17019
41. Nucifora Jr. F.C., Sasaki M., Peters M.F., Huang H., Cooper J.K., Yamada M., Takahashi H., Tsuji S., Troncoso J., Dawson V.L., Dawson T.M., and Ross C.A. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291 (2001) 2423-2428
42. Chen S., Berthelier V., Yang W., and Wetzel R. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311 (2001) 173-182
43. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
44. Vuilleumier S. Bacterial glutathione S-transferases: what are they good for?. J. Bacteriol. 179 (1997) 1431-1441
45. Rossjohn J., Board P.G., Parker M.W., and Wilce M.C. A structurally derived consensus pattern for theta class glutathione transferases. Protein Eng. 9 (1996) 327-332
46. Rossjohn J., Polekhina G., Feil S.C., Allocati N., Masulli M., De I.C., and Parker M.W. A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6 (1998) 721-734
47. Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
48. Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10 (1997) 2-18
49. Mannervik B., Cameron A.D., Fernandez E., Gustafsson A., Hansson L.O., Jemth P., Jiang F., Jones T.A., Larsson A.K., Nilsson L.O., Olin B., Pettersson P.L., Ridderstrom M., Stenberg G., and Widersten M. An evolutionary approach to the design of glutathione-linked enzymes. Chem. Biol. Interact. 111-112 (1998) 15-21
50. Saito Y., Hayashi T., Tanaka A., Watanabe Y., Suzuki M., Saito E., and Takahashi K. Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein P. J. Biol. Chem. 274 (1999) 2866-2871
51. Nay B., Fournier D., Baudras A., and Baudras B. Mechanism of an insect glutathione S-transferase: kinetic analysis supporting a rapid equilibrium random sequential mechanism with housefly I1 isoform. Insect Biochem. Mol. Biol. 29 (1999) 71-79
52. Labrou N.E., Mello L.V., and Clonis Y.D. Functional and structural roles of the glutathione-binding residues in maize (Zea mays) glutathione S-transferase I. Biochem. J. 358 (2001) 101-110
53. Caccuri A.M., Antonini G., Allocati N., Di I.C., De M.F., Innocenti F., Parker M.W., Masulli M., Lo B.M., Turella P., Federici G., and Ricci G. GSTB1-1 from Proteus mirabilis: a snapshot of an enzyme in the evolutionary pathway from a redox enzyme to a conjugating enzyme. J. Biol. Chem. 277 (2002) 18777-18784
54. Choi J.H., Lou W., and Vancura A. A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 29915-29922
55. Collinson E.J., and Grant C.M. Role of yeast glutaredoxins as glutathione S-transferases. J. Biol. Chem. 278 (2003) 22492-22497
56. Avery A.M., and Avery S.V. Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases. J. Biol. Chem. 276 (2001) 33730-33735
57. Nilsson L.O., Gustafsson A., and Mannervik B. Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9408-9412
58. Bousset L., Belrhali H., Janin J., Melki R., and Morera S. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9 (2001) 39-46
59. Bousset L., Belrhali H., Melki R., and Morera S. Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40 (2001) 13564-13573
60. Rai R., Tate J.J., and Cooper T.G. Ure2, a prion precursor with homology to glutathione S-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity. J. Biol. Chem. 278 (2003) 12826-12833
61. Rai R., and Cooper T.G. In vivo specificity of Ure2 protection from heavy metal ion and oxidative cellular damage in Saccharomyces cerevisiae. Yeast 22 (2005) 343-358
62. Basu U., Southron J.L., Stephens J.L., and Taylor G.J. Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of PHGPX and URE2 genes in aluminum resistance in Saccharomyces cerevisiae. Mol. Genet. Genomics 271 (2004) 627-637
63. Fraser J.A., Davis M.A., and Hynes M.J. 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. Appl. Environ. Microbiol. 68 (2002) 2802-2808
64. Bai M., Zhou J.M., and Perrett S. The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J. Biol. Chem. 279 (2004) 50025-50030
65. Aigle M., and Lacroute F. Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol. Gen. Genet. 136 (1975) 327-335
66. Nakayashiki T., Kurtzman C.P., Edskes H.K., and Wickner R.B. Yeast prions [URE3] and [PSI+] are diseases. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 10575-10580
67. Baudin-Baillieu A., Fernandez-Bellot E., Reine F., Coissac E., and Cullin C. Conservation of the prion properties of Ure2p through evolution. Mol. Biol. Cell 14 (2003) 3449-3458
68. Talarek N., Maillet L., Cullin C., and Aigle M. The [URE3] prion is not conserved among Saccharomyces species. Genetics 171 (2005) 23-24
69. Masison D.C., Maddelein M.L., and Wickner R.B. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12503-12508
70. Edskes H.K., and Wickner R.B. Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl. 4 (2002) 16384-16391
71. Ross E.D., Baxa U., and Wickner R.B. Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 24 (2004) 7206-7213
72. Maddelein M.L., and Wickner R.B. Two prion-inducing regions of Ure2p are nonoverlapping. Mol. Cell. Biol. 19 (1999) 4516-4524
73. Fernandez-Bellot E., Guillemet E., and Cullin C. The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J. 19 (2000) 3215-3222
74. Walter S., and Buchner J. Molecular chaperones-Cellular machines for protein folding. Angew. Chem., Int. Ed. Engl. 41 (2002) 1098-1113
75. Young J.C., Agashe V.R., Siegers K., and Hartl F.U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev., Mol. Cell. Biol. 5 (2004) 781-791
76. Jones G.W., and Tuite M.F. Chaperoning prions: the cellular machinery for propagating an infectious protein?. Bioessays 27 (2005) 823-832
77. Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., and Liebman S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268 (1995) 880-884
78. Moriyama H., Edskes H.K., and Wickner R.B. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20 (2000) 8916-8922
79. Grimminger V., Richter K., Imhof A., Buchner J., and Walter S. The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J. Biol. Chem. 279 (2004) 7378-7383
80. Eaglestone S.S., Ruddock L.W., Cox B.S., and Tuite M.F. Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 240-244
81. Jung G., Jones G., and Masison D.C. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9936-9941
82. Kushnirov V.V., and Ter-Avanesyan M.D. Structure and replication of yeast prions. Cell 94 (1998) 13-16
83. Wegrzyn R.D., Bapat K., Newnam G.P., Zink A.D., and Chernoff Y.O. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol. Cell. Biol. 21 (2001) 4656-4669
84. Ness F., Ferreira P., Cox B.S., and Tuite M.F. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol. Cell. Biol. 22 (2002) 5593-5605
85. Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., and Kushnirov V.V. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278 (2003) 49636-49643
86. Shorter J., and Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304 (2004) 1793-1797
87. Glover J.R., and Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 (1998) 73-82
88. Diamant S., Ben-Zvi A.P., Bukau B., and Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275 (2000) 21107-21113
89. Schwimmer C., and Masison D.C. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol. Cell. Biol. 22 (2002) 3590-3598
90. Roberts B.T., Moriyama H., and Wickner R.B. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21 (2004) 107-117
91. Jones G., Song Y., Chung S., and Masison D.C. Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol. Cell. Biol. 24 (2004) 3928-3937
92. Jones G.W., and Masison D.C. Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]. Genetics 163 (2003) 495-506
93. Newnam G.P., Wegrzyn R.D., Lindquist S.L., and Chernoff Y.O. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19 (1999) 1325-1333
94. Lopez N., Aron R., and Craig E.A. Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. Mol. Biol. Cell 14 (2003) 1172-1181
95. Bradley M.E., Edskes H.K., Hong J.Y., Wickner R.B., and Liebman S.W. Interactions among prions and prion "strains" in yeast. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl. 4 (2002) 16392-16399
96. Kushnirov V.V., Kryndushkin D.S., Boguta M., Smirnov V.N., and Ter-Avanesyan M.D. Chaperones that cure yeast artificial [PSI+] and their prion-specific effects. Curr. Biol. 10 (2000) 1443-1446
97. Sakahira H., Breuer P., Hayer-Hartl M.K., and Hartl F.U. Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl. 4 (2002) 16412-16418
98. Gokhale K.C., Newnam G.P., Sherman M.Y., and Chernoff Y.O. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem. 280 (2005) 22809-22818
99. Griffith J.S. Self-replication and scrapie. Nature 215 (1967) 1043-1044
100. Harper J.D., and Lansbury Jr. P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
101. Kelly J.W. Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7 (2000) 824-826
102. Fay N., Inoue Y., Bousset L., Taguchi H., and Melki R. Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization. J. Biol. Chem. 278 (2003) 30199-30205
103. Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., Arnsdorf M.F., and Lindquist S.L. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289 (2000) 1317-1321
104. Bousset L., Redeker V., Decottignies P., Dubois S., Le M.P., and Melki R. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry 43 (2004) 5022-5032
105. Zhou J.M., Zhu L., Balny C., and Perrett S. Pressure denaturation of the yeast prion protein Ure2. Biochem. Biophys. Res. Commun. 287 (2001) 147-152
106. Fernandez-Bellot E., Guillemet E., Baudin-Baillieu A., Gaumer S., Komar A.A., and Cullin C. Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. Biochem. J. 338 Pt. 2 (1999) 403-407
107. Pierce M.M., Baxa U., Steven A.C., Bax A., and Wickner R.B. Is the prion domain of soluble Ure2p unstructured?. Biochemistry 44 (2005) 321-328
108. Rochet J.C., and Lansbury Jr. P.T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10 (2000) 60-68
109. Schlumpberger M., Wille H., Baldwin M.A., Butler D.A., Herskowitz I., and Prusiner S.B. The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein. Protein Sci. 9 (2000) 440-451
110. Baxa U., Speransky V., Steven A.C., and Wickner R.B. Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 5253-5260
111. Perrett S., and Zhou J.M. Expanding the pressure technique: insights into protein folding from combined use of pressure and chemical denaturants. Biochim. Biophys. Acta 1595 (2002) 210-223
112. Zhu L., Kihara H., Kojima M., Zhou J.M., and Perrett S. Small angle X-ray scattering study of the yeast prion Ure2p. Biochem. Biophys. Res. Commun. 311 (2003) 525-532
113. Bousset L., Thomson N.H., Radford S.E., and Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21 (2002) 2903-2911
114. Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., and Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89 (1997) 811-819
115. Kong C., Ito K., Walsh M.A., Wada M., Liu Y., Kumar S., Barford D., Nakamura Y., and Song H. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol. Cell 14 (2004) 233-245
116. Sulkowski E. Spontaneous conversion of PrPC to PrPSc. FEBS Lett. 307 (1992) 129-130
117. Viles J.H., Cohen F.E., Prusiner S.B., Goodin D.B., Wright P.E., and Dyson H.J. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 2042-2047
118. Stockel J., Safar J., Wallace A.C., Cohen F.E., and Prusiner S.B. Prion protein selectively binds copper(II) ions. Biochemistry 37 (1998) 7185-7193
119. Humphrey W., Dalke A., and Schulten K. VMD: visual molecular dynamics. J. Mol. Graph. 14 (1996) 33-38
120. Edskes H.K., Gray V.T., and Wickner R.B. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 1498-1503