Amyloids and yeast prion biology

Biochemistry

Volumn 52, Issue 9, 2013, Pages 1514-1527

  Wickner, Reed B ^a   Edskes, Herman K ^a   Bateman, David A ^a   Kelly, Amy C ^a   Gorkovskiy, Anton ^a   Dayani, Yaron ^a   Zhou, Albert ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID DISEASE; CELLULAR COMPONENTS; DNA TEMPLATING; ITS SEQUENCES; PROTEIN SEQUENCES; SELF-PROPAGATING; SHEET STRUCTURE; SOLUBLE PROTEINS; STRUCTURAL BASIS; TEMPLATING; YEAST PRIONS;

CONFORMATIONS; GENES; GLYCOPROTEINS; YEAST;

PROTEINS;

AMYLOID; FUNGAL DNA; PRION PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; DNA TEMPLATE; FUNGAL GENETICS; NONHUMAN; PODOSPORA ANSERINA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; YEAST;

AMINO ACID SEQUENCE; AMYLOID; FUNGAL PROTEINS; FUNGI; GENES, FUNGAL; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PRIONS; PROTEIN CONFORMATION;

EID: 84874597470     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301686a     Document Type: Article

References (187)

1. Griffith, J. S. (1967) Self-replication and scrapie Nature 215, 1043-1044
2. Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie Science 216, 136-144 (Pubitemid 12089840)
3. Kim, J.-I., Cali, I., Surewicz, K., Kong, Q., Raymond, G. J., Atarashi, R., Race, B., Qing, L., Gambetti, P., Caughey, B., and Surewicz, W. K. (2010) Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors J. Biol. Chem. 285, 14083-14087
4. Delault, N. R., Piro, J. R., Walsh, D. J., Wang, F., Ma, J., Geoghegan, J. C., and Supattapone, S. (2012) Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids Proc. Natl. Acad. Sci. U.S.A. 109, 8546-8551
5. Cox, B. S. (1965) PSI, a cytoplasmic suppressor of super-suppressor in yeast Heredity 20, 505-521
6. Lacroute, F. (1971) Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast J. Bacteriol. 106, 519-522
7. Wickner, R. B. (1994) [URE3] as an altered URE2 protein: Evidence for a prion analog in S. cerevisiae Science 264, 566-569 (Pubitemid 24185861)
8. Wickner, R. B., Shewmaker, F., Edskes, H., Kryndushkin, D., Nemecek, J., McGlinchey, R., Bateman, D., and Winchester, C.-L. (2010) Prion amyloid structure explains templating: How proteins can be genes FEMS Yeast Res. 10, 980-991
9. Wickner, R. B., Edskes, H. K., Kryndushkin, D. S., McGlinchey, R., Bateman, D., and Kelly, A. (2011) Prion diseases of yeast: Amyloid structure and biology Semin. Cell Dev. Biol. 22, 469-475
10. 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 (Pubitemid 24196460)
11. 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
12. 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. U.S.A. 94, 12503-12508 (Pubitemid 27492558)
13. Balguerie, A., Dos Reis, S., Ritter, C., Chaignepain, S., Coulary-Salin, B., Forge, V., Bathany, K., Lascu, I., Schmitter, J.-M., Riek, R., and Saupe, S. (2003) Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina EMBO J. 22, 2071-2081 (Pubitemid 36565532)
14. Suzuki, G., Shimazu, N., and Tanaka, M. (2012) A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress Science 336, 355-359
15. Shewmaker, F., Mull, L., Nakayashiki, T., Masison, D. C., and Wickner, R. B. (2007) Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae Genetics 176, 1557-1565 (Pubitemid 47105217)
16. Kobayashi, T., Funakoshi, Y., Hoshino, S., and Katada, T. (2004) The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay J. Biol. Chem. 279, 45693-45700 (Pubitemid 39491558)
17. +] determinant in Saccharmyces cerevisiae Curr. Genet. 34, 146-151 (Pubitemid 28431878)
18. +] determinant is mediated by oligomerization of the SUP35 -encoded polypeptide chain release factor EMBO J. 15, 3127-3134 (Pubitemid 26187760)
19. 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 (Pubitemid 26262109)
20. 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. U.S.A. 96, 1498-1503 (Pubitemid 29098479)
21. 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. U.S.A. 94, 6618-6622 (Pubitemid 27281913)
22. 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 (Pubitemid 27450712)
23. 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 (Pubitemid 27516184)
24. 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
25. Caston, J. R., Trus, B. L., Booy, F. P., Wickner, R. B., Wall, J. S., and Steven, A. C. (1997) Structure of L-A virus: A specialized compartment for the transcription and replication of double-stranded RNA J. Cell Biol. 138, 975-985 (Pubitemid 27386449)
26. Kawai-Noma, S., Pack, C. G., Kojidani, T., Asakawa, H., Hiraoka, Y., Kinjo, M., Haraguchi, T., Taguchi, H., and Hirata, A. (2010) In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells J. Cell Biol. 190, 223-231
27. King, C. Y. and Diaz-Avalos, R. (2004) Protein-only transmission of three yeast prion strains Nature 428, 319-323 (Pubitemid 38418802)
28. Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J. S. (2004) Conformational variations in an infectious protein determine prion strain differences Nature 428, 323-328 (Pubitemid 38418803)
29. Brachmann, A., Baxa, U., and Wickner, R. B. (2005) Prion generation in vitro: Amyloid of Ure2p is infectious EMBO J. 24, 3082-3092 (Pubitemid 41486344)
30. Collins, S. R., Douglass, A., Vale, R. D., and Weissman, J. S. (2004) Mechanism of prion propagation: Amyloid growth occurs by monomer addition PLoS Biol. 2, 1582-1590
31. Scheibel, T., Kowal, A. S., Bloom, J. D., and Lindquist, S. L. (2001) Bidirectional amyloid fiber growth for a yeast prion determinant Curr. Biol. 11, 366-369 (Pubitemid 32200741)
32. Inoue, Y., Kishimoto, A., Hirao, J., Yoshida, M., and Taguchi, H. (2001) Strong growth polarity of yeast prion fiber revealed by single fiber imaging J. Biol. Chem. 276, 35227-35230
33. Zubenko, G. S., Park, F. J., and Jones, E. W. (1982) Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae Genetics 102, 679-690
34. Roberts, B. T. and Wickner, R. B. (2003) A class of prions that propagate via covalent auto-activation Genes Dev. 17, 2083-2087
35. Ball, A. J. S., Wong, D. K., and Elliott, J. J. (1976) Glucosamine resistance in yeast I. A preliminary genetic analysis Genetics 84, 311-317
36. Brown, J. C. and Lindquist, S. (2009) A heritable switch in carbon source utilization driven by an unusual yeast prion Genes Dev. 23, 2320-2332
37. Coustou, V., Deleu, C., Saupe, S., and Begueret, J. (1997) 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, 9773-9778 (Pubitemid 27408139)
38. Saupe, S. J. (2011) The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility Semin. Cell Dev. Biol. 22, 460-468
39. Maddelein, M. L., Dos Reis, S., Duvezin-Caubet, S., Coulary-Salin, B., and Saupe, S. J. (2002) Amyloid aggregates of the HET-s prion protein are infectious Proc. Natl. Acad. Sci. U.S.A. 99, 7402-7407 (Pubitemid 34568703)
40. 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 (Pubitemid 27418562)
41. Sondheimer, N. and Lindquist, S. (2000) Rnq1: An epigenetic modifier of protein function in yeast Mol. Cell 5, 163-172 (Pubitemid 30105445)
42. Derkatch, I. L., Bradley, M. E., Hong, J. Y., and Liebman, S. W. (2001) Prions affect the appearance of other prions: The story of [PIN] Cell 106, 171-182 (Pubitemid 32772628)
43. Osherovich, L. Z. and Weissman, J. S. (2001) Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion Cell 106, 183-194 (Pubitemid 32772629)
44. Du, Z., Park, K.-W., Yu, H., Fan, Q., and Li, L. (2008) Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae Nat. Genet. 40, 460-465 (Pubitemid 351450881)
45. Patel, B. K., Gavin-Smyth, J., and Liebman, S. W. (2009) The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion Nat. Cell Biol. 11, 344-349
46. Volkov, K. V., Aksenova, Y. A., Soom, M. J., Sipov, K. V., Svitin, A. V., Kurischko, C., Shkundina, I. S., Ter-Avanesyan, M. D., Inge-Vechtomov, S. G., and Mironova, L. N. (2002) Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae Genetics 160, 25-36 (Pubitemid 34118268)
47. Rogoza, T., Goginashvili, A., Rodionova, S., Ivanov, M., Viktorovskaya, O., Rubel, A., Volkov, K., and Mironova, L. (2010) Non-mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1 Proc. Natl. Acad. Sci. U.S.A. 107, 10573-10577
48. Marion, R. M., Regev, A., Segal, E., Barash, Y., Koller, D., Friedman, N., and O'Shea, E. K. (2004) Sfp1 is a stress-and nutrient-sensitive regulator of ribosomal protein gene expression Proc. Natl. Acad. Sci. U.S.A. 101, 14315-14322 (Pubitemid 39346746)
49. Rogoza, R. E., Khokhrina, M., Drozdova, P., and Mironova, L. (2011) SUP35 expression is enhanced in yeast containing [ISP+], a prion form of the transcription regulator Sfp1 Prion 5, 317-322
50. Dihanich, M. E., Najarian, D., Clark, R., Gillman, E. C., Martin, N. C., and Hopper, A. K. (1987) Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae Mol. Cell. Biol. 7, 177-184 (Pubitemid 17230397)
51. Alberti, S., Halfmann, R., King, O., Kapila, A., and Lindquist, S. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137, 146-158
52. Hongay, C., Jia, N., Bard, M., and Winston, F. (2002) Mot3 is a transcriptional repressor of ergosterol biosynthetic genes and is required for normal vacuolar function in Saccharomyces cerevisiae EMBO J. 21, 4114-4124 (Pubitemid 34857443)
53. Yoshikawa, K., Tanaka, T., Ida, Y., Furusawa, C., and Hirasawa, T. (2011) Comprehensive phenotypic analysis of single-gene deletion and overexpression strains of Saccharomyces cerevisiae Yeast 28, 349-361
54. Merz, S. and Westermann, B. (2009) Genome-wide deletion mutant analysis reveals genes required for respiratory growth, mitochondrial genome maintenance and mitochondrial protein synthesis in Saccharomyces cerevisiae Genome Biol. 10, R95
55. 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 (Pubitemid 26427888)
56. +] and their prion-specific effects Curr. Biol. 10, 1443-1446 (Pubitemid 32692874)
57. Bradley, M. E. and Liebman, S. W. (2003) Destabilizing interactions among [ PSI+ ] and [ PIN+ ] yeast prion variants Genetics 165, 1675-1685 (Pubitemid 38040262)
58. Borchsenius, A. S., Muller, S., Newnam, G. P., Inge-Vechtomov, S. G., and Chernoff, Y. O. (2006) Prion variant maintained only at high levels of the Hsp104 disaggregase Curr. Genet. 49, 21-29 (Pubitemid 43118774)
59. Kryndushkin, D., Shewmaker, F., and Wickner, R. B. (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein EMBO J. 27, 2725-2735
60. Vishveshwara, N. and Liebman, S. W. (2009) Heterologous cross-seeding mimics cross-species prion conversion in a yeast model BMC Biol. 7, 26
61. Edskes, H. K., McCann, L. M., Hebert, A. M., and Wickner, R. B. (2009) Prion variants and species barriers among Saccharomyces Ure2 proteins Genetics 181, 1159-1167
62. Bateman, D. and Wickner, R. B. (2013) The [PSI+] prion exists as a dynamic cloud of variants PLoS Genet. e1003257
63. Chang, H.-Y., Lin, J.-Y., Lee, H.-C., Wang, H.-L., and King, C.-Y. (2008) Strain-specific sequences required for yeast prion [PSI+] propagation Proc. Natl. Acad. Sci. U.S.A. 105, 13345-13350
64. Ross, E. D., Baxa, U., and Wickner, R. B. (2004) Scrambled prion domains form prions and amyloid Mol. Cell. Biol. 24, 7206-7213 (Pubitemid 39014446)
65. Ross, E. D., Edskes, H. K., Terry, M. J., and Wickner, R. B. (2005) Primary sequence independence for prion formation Proc. Natl. Acad. Sci. U.S.A. 102, 12825-12830 (Pubitemid 41279450)
66. Toombs, J. A., Liss, N. M., Cobble, K. R., Ben-Musa, Z., and Ross, E. D. (2011) [PSI] maintenance is dependent on the composition, not the primary sequence, of the oligopeptide repeat domain PLoS One 6, e21953
67. Parham, S. N., Resende, C. G., and Tuite, M. F. (2001) Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions EMBO J. 20, 2111-2119 (Pubitemid 32410581)
68. Toombs, J. A., McCarty, B. R., and Ross, E. D. (2010) Compositional determinants of prion formation in yeast Mol. Cell. Biol. 30, 319-332
69. Toombs, J. A., Petri, M., Paul, K. R., Kan, G. Y., and Ross, E. D. (2012) De novo design of synthetic prion domains Proc. Natl. Acad. Sci. U.S.A. 109, 6519-6524
70. Ross, E. D., Minton, A. P., and Wickner, R. B. (2005) Prion domains: Sequences, structures and interactions Nat. Cell Biol. 7, 1039-1044
71. Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin Nature 410, 165-166
72. Patel, B. K. and Liebman, S. W. (2007) "Prion proof" for [PIN+]: Infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+] J. Mol. Biol. 365, 773-782 (Pubitemid 44960370)
73. Tycko, R. (2011) Solid-state NMR studies of amyloid fibril structure Annu. Rev. Phys. Chem. 62, 279-299
74. Tycko, R. (2006) Molecular structure of amyloid fibrils: Insights from solid-state NMR Q. Rev. Biophys. 1, 1-55 (Pubitemid 44566373)
75. Benzinger, T. L., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., and Meredith, S. C. (1998) Propagating structure of Alzheimer's β-amyloid(10-35) is parallel β-sheet with residues in exact register Proc. Natl. Acad. Sci. U.S.A. 95, 13407-13412
76. Shewmaker, F., Wickner, R. B., and Tycko, R. (2006) Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure Proc. Natl. Acad. Sci. U.S.A. 103, 19754-19759 (Pubitemid 46037503)
77. Baxa, U., Wickner, R. B., Steven, A. C., Anderson, D., Marekov, L., Yau, W.-M., and Tycko, R. (2007) Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance Biochemistry 46, 13149-13162 (Pubitemid 350086233)
78. +] prion, has a parallel in-register β-sheet structure Proc. Natl. Acad. Sci. U.S.A. 105, 2403-2408 (Pubitemid 351520526)
79. Kryndushkin, D. S., Wickner, R. B., and Tycko, R. (2011) The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: Evidence from solid-state NMR J. Mol. Biol. 409, 263-277
80. Ngo, S., Gu, L., and Guo, Z. (2011) Hierarchical organization in the amyloid core of yeast prion protein Ure2 J. Biol. Chem. 286, 29691-29699
81. Shewmaker, F., Kryndushkin, D., Chen, B., Tycko, R., and Wickner, R. B. (2009) Two prion variants of Sup35p have in-register β-sheet structures, independent of hydration Biochemistry 48, 5074-5082
82. Bradley, M. E. and Liebman, S. W. (2004) The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions Mol. Microbiol. 51, 1649-1659 (Pubitemid 38406539)
83. Toyama, B. H., Kelly, M. J., Gross, J. D., and Weissman, J. S. (2007) The structural basis of yeast prion strain variants Nature 449, 233-237 (Pubitemid 47402368)
84. Bateman, D. A. and Wickner, R. B. (2012) [PSI+] prion transmission barriers protect Saccharomyces cerevisiae from infection: Intraspecies 'species barriers' Genetics 190, 569-579
85. Baxa, U., Taylor, K. L., Wall, J. S., Simon, M. N., Cheng, N., Wickner, R. B., and Steven, A. (2003) Architecture of Ure2p prion filaments: The N-terminal domain forms a central core fiber J. Biol. Chem. 278, 43717-43727 (Pubitemid 37345999)
86. Diaz-Avalos, R., King, C. Y., Wall, J. S., Simon, M., and Caspar, D. L. D. (2005) Strain-specific morphologies of yeast prion amyloids Proc. Natl. Acad. Sci. U.S.A. 102, 10165-10170 (Pubitemid 41023343)
87. Chen, B., Thurber, K. R., Shewmaker, F., Wickner, R. B., and Tycko, R. (2009) Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy Proc. Natl. Acad. Sci. U.S.A. 106, 14339-14344
88. Sen, A., Baxa, U., Simon, M. N., Wall, J. S., Sabate, R., Saupe, S. J., and Steven, A. C. (2006) Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked β-solenoid model of HET-s prion fibrils J. Biol. Chem. 282, 5545-5550 (Pubitemid 47093734)
89. Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 105, 18349-18354
90. Bousset, L., Thomson, N. H., Radford, S. E., and Melki, R. (2002) The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro EMBO J. 21, 2903-2911 (Pubitemid 34670375)
91. Bousset, L., Briki, F., Doucet, J., and Melki, R. (2003) The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils J. Struct. Biol. 141, 132-140
92. Pierce, M. M., Baxa, U., Steven, A. C., Bax, A., and Wickner, R. B. (2005) Is the prion domain of soluble Ure2p unstructured? Biochemistry 44, 321-328 (Pubitemid 40095734)
93. Baxa, U., Cheng, N., Winkler, D. C., Chiu, T. K., Davies, D. R., Sharma, D., Inouye, H., Kirschner, D. A., Wickner, R. B., and Steven, A. C. (2005) Filaments of the Ure2p prion protein have a cross-β core structure J. Struct. Biol. 150, 170-179 (Pubitemid 40615742)
94. Thual, C., Komar, A. A., Bousset, L., Fernandez-Bellot, E., Cullin, C., and Melki, R. (1999) Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2 J. Biol. Chem. 274, 13666-13674
95. Jiang, Y., Li, H., Zhu, L., Zhou, J. M., and Perrett, S. (2004) Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and non-repeat regions of the prion domains J. Biol. Chem. 279, 3361-3369 (Pubitemid 38140571)
96. Loquet, A., Bousset, L., Gardiennet, C., Sourigues, Y., Wasmer, C., Habenstein, B., Schutz, A., Meier, B. H., and Melki, R. (2009) Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded molecules J. Mol. Biol. 394, 108-118
97. Krishnan, R. and Lindquist, S. (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity Nature 435, 765-772 (Pubitemid 40839721)
98. Tycko, R. and Wickner, R. B. Molecular structures of amyloid and prion fibrils: Consensus versus controversy. Acc. Chem. Res. 2013, in press.
99. Glover, J. R. and Lindquist, S. (1998) Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins Cell 94, 73-82 (Pubitemid 28347471)
100. 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. 43, 7-10 (Pubitemid 32549917)
101. Ferreira, P. C., Ness, F., Edwards, S. R., Cox, B. S., and Tuite, M. F. (2001) The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation Mol. Microbiol. 40, 1357-1369 (Pubitemid 32635304)
102. Jung, G., Jones, G., and Masison, D. C. (2002) 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, 9936-9941 (Pubitemid 34831151)
103. +] Science 268, 880-884
104. 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 (Pubitemid 32245922)
105. Ness, F., Ferreira, P., Cox, B. S., and Tuite, M. F. (2002) Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast Mol. Cell. Biol. 22, 5593-5605 (Pubitemid 34755768)
106. Cox, B. S., Ness, F., and Tuite, M. F. (2003) Analysis of the generation and segregation of propagons: Entities that propagate the [PSI+] prion in yeast Genetics 165, 23-33 (Pubitemid 37204053)
107. +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104 J. Biol. Chem. 278, 49636-49643
108. Reidy, M. and Masison, D. C. (2011) Modulation and elimination of yeast prions by protein chaperones and co-chaperones Prion 5, 245-249
109. Inoue, Y., Taguchi, H., Kishimoto, A., and Yoshida, M. (2004) Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it J. Biol. Chem. 279, 52319-52323 (Pubitemid 39656606)
110. Krzewska, J., Tanaka, M., Burston, S. G., and Melki, R. (2007) Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain J. Biol. Chem. 282, 1679-1686 (Pubitemid 47076690)
111. Helsen, C. W. and Glover, J. R. (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104) J. Biol. Chem. 287, 542-556
112. Reidy, M. and Masison, D. C. (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions Genetics 192, 185-193
113. Lum, R., Tkach, J. M., Vierling, E., and Glover, J. R. (2004) Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104 J. Biol. Chem. 279, 29139-29146 (Pubitemid 38915786)
114. Tessarz, P., Mogk, A., and Bukau, B. (2008) Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation Mol. Microbiol. 68, 87-97 (Pubitemid 351372041)
115. Hung, G. C. and Masison, D. C. (2006) N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression Genetics 173, 611-620 (Pubitemid 43945883)
116. Higurashi, T., Hines, J. K., Sahi, C., Aron, R., and Craig, E. A. (2008) Specificity of the J-protein Sis1 in the propagation of 3 yeast prions Proc. Natl. Acad. Sci. U.S.A. 105, 16596-16601
117. Kirkland, P. A., Reidy, M., and Masison, D. C. (2011) Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity Genetics 188, 565-577
118. Allen, K. D., Chernova, T. A., Tennant, E. P., Wilkinson, K. D., and Chernoff, Y. O. (2007) Effects of ubiquitin system alterations on the formation and loss of a yeast prion J. Biol. Chem. 282, 3004-3013 (Pubitemid 47084312)
119. Reidy, M. and Masison, D. C. (2010) Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104 Mol. Cell. Biol. 30, 3542-3552
120. Moosavi, B., Wongwigkam, J., and Tuite, M. F. (2010) Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI+] prion but not for prion propagation Yeast 27, 167-179
121. Kryndushkin, D. S., Engel, A., Edskes, H. K., and Wickner, R. B. (2011) Molecular chaperone Hsp104 can promote yeast prion generation Genetics 188, 339-348
122. Aguilaniu, H., Gustafsson, L., Gigoulet, M., and Nystrom, T. (2003) Assymetric inheritance of oxidatively damaged proteins during cytokinesis Science 299, 1751-1753 (Pubitemid 36337204)
123. Kaeberlein, M., McVey, M., and Guarente, L. (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms Genes Dev. 13, 2570-2580 (Pubitemid 29489648)
124. Erjavec, N., Larsson, L., Grantham, J., and Nystrom, T. (2007) Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p Genes Dev. 21, 2410-2421 (Pubitemid 47529371)
125. Shewmaker, F. and Wickner, R. B. (2006) Aging in yeast does not enhance prion generation Yeast 23, 1123-11128
126. Kampinga, H. H. and Craig, E. A. (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity Nat. Rev. Mol. Cell Biol. 11, 759-592
127. 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 (Pubitemid 29046874)
128. 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
129. Roberts, B. T., Moriyama, H., and Wickner, R. B. (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast Yeast 21, 107-117 (Pubitemid 38219964)
130. Schwimmer, C. and Masison, D. C. (2002) 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, 3590-3598 (Pubitemid 34525203)
131. Sharma, D. and Masison, D. C. (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p Proc. Natl. Acad. Sci. U.S.A. 108, 13665-13670
132. 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 (Pubitemid 30414005)
133. Pearce, D. A., Ferea, T., Nosel, S. A., Das, B., and Sherman, F. (1999) Action of BTN1, the yeast ortholog of the gene mutated in Batten disease Nat. Genet. 22, 55-58 (Pubitemid 29214804)
134. Malinovska, L., Kroschwald, S., Munder, M. C., Richter, D., and Alberti, S. (2012) Molecular chaperones and stress-inducible protein-sorting factors coordinate the spaciotemporal distribution of protein aggregates Mol. Biol. Cell 23, 3041-3056
135. Chattopadhyay, S., Muzaffar, N. E., Sherman, F., and Pearce, D. A. (2000) The yeast model for batten disease: Mutations in BTN1, BTN2, and HSP30 alter pH homeostasis J. Bacteriol. 182, 6418-6423
136. Kama, R., Robinson, M., and Gerst, J. E. (2007) Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast Mol. Cell. Biol. 27, 605-621 (Pubitemid 46080128)
137. Chattopadhyay, S., Roberts, P. M., and Pearce, D. A. (2003) The yeast model for Batten disease: A role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p Biochem. Biophys. Res. Commun. 302, 534-538 (Pubitemid 36279563)
138. Kaganovich, D., Kopito, R., and Frydman, J. (2008) Misfolded proteins partition between two distinct quality control compartments Nature 454, 1088-1095
139. Specht, S., Miller, S. B. M., Mogk, A., and Bukau, B. (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae J. Cell Biol. 195, 617-629
140. Kryndushkin, D., Ihrke, G., Piermartiri, T. C., and Shewmaker, F. (2012) A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity Mol. Microbiol. 86, 1531-1547
141. Wickner, R. B. (1997) A new prion controls fungal cell fusion incompatibility Proc. Natl. Acad. Sci. U.S.A. 94, 10012-10014 (Pubitemid 27406984)
142. Eaglestone, S. S., Cox, B. S., and Tuite, M. F. (1999) Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism EMBO J. 18, 1974-1981 (Pubitemid 29158540)
143. True, H. L. and Lindquist, S. L. (2000) A yeast prion provides a mechanism for genetic variation and phenotypic diversity Nature 407, 477-483
144. +] Nat. Cell Biol. 10, 1069-1075
145. Tyedmers, J., Madariaga, M. L., and Lindquist, S. (2008) Prion switching in response to environmental stress PLoS Biol. 6, e294
146. Kelly, A. C., Shewmaker, F. P., Kryndushkin, D., and Wickner, R. B. (2012) Sex, prions and plasmids in yeast Proc. Natl. Acad. Sci. U.S.A. 109, E2683-E2690
147. Saunders, S. E., Bartelt-Hunt, S. L., and Bartz, J. C. (2012) Occurence, transmission, and zoonotic potential of chronic wasting disease Emerging Infect. Dis. 18, 369-376
148. +] are diseases Proc. Natl. Acad. Sci. U.S.A. 102, 10575-10580 (Pubitemid 41061596)
149. Halfmann, R., Jarosz, D. F., Jones, S. K., Chang, A., Lancster, A. K., and Lindquist, S. (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts Nature 482, 363-368
150. Tsai, I. J., Bensasson, D., Burt, A., and Koufopanou, V. (2008) Population genomics of the wild yeast Saccharomyces paradoxus: Quantifying the life cycle Proc. Natl. Acad. Sci. U.S.A. 105, 4957-4962 (Pubitemid 351753853)
151. Ruderfer, D. M., Pratt, S. C., Seidel, H. S., and Kruglyak, L. (2006) Population genomic analysis of outcrossing and recombination in yeast Nat. Genet. 38, 1077-1081 (Pubitemid 44325936)
152. Futcher, A. B. and Cox, B. S. (1983) Maintenance of the 2 μm circle plasmid in populations of Saccharomyces cerevisiae J. Bacteriol. 154, 612-622 (Pubitemid 13080996)
153. Futcher, B., Reid, E., and Hickey, D. A. (1988) Maintenance of the 2 micron circle plasmid of Saccharomyces cerevisiae by sexual transmission: An example of selfish DNA Genetics 118, 411-415 (Pubitemid 18087674)
154. Mead, D. J., Gardner, D. C. J., and Oliver, S. G. (1986) The yeast 2 μ plasmid: Strategies for the survival of a selfish DNA Mol. Gen. Genet. 205, 417-421 (Pubitemid 17038603)
155. Debets, A. J., Dalstra, H. J., Slakhorst, M., Koopmanschap, B., Hoekstra, R. F., and Saupe, S. J. (2012) High natural prevalence of a fungal prion Proc. Natl. Acad. Sci. U.S.A. 109, 10432-10437
156. Dalstra, H. J. P., Swart, K., Debets, A. J. M., Saupe, S. J., and Hoekstra, R. F. (2003) Sexual transmission of the [Het-s] prion leads to meiotic drive in Podospora anserina Proc. Natl. Acad. Sci. U.S.A. 100, 6616-6621 (Pubitemid 36666630)
157. McGlinchey, R., Kryndushkin, D., and Wickner, R. B. (2011) Suicidal [PSI+] is a lethal yeast prion Proc. Natl. Acad. Sci. U.S.A. 108, 5337-5341
158. Klucevsek, K. M., Braun, M. A., and Arndt, K. M. (2012) The Paf1 complex subunit Rtf1 buffers cells against the toxic effects of [PSI+] and defects in Rkr1-dependent protein quality control in Saccharomyces cerevisiae Genetics 191, 1107-1118
159. Gunasova, E. E., Ozolins, L. N., Bhagat, S., Newnam, G. P., Wegrzyn, R. D., Sherman, M. Y., and Chernoff, Y. O. (2006) Modulation of prion formation,
160. Vishveshwara, N., Bradley, M. E., and Liebman, S. W. (2009) Sequestration of essential proteins causes prion associated toxicity in yeast Mol. Microbiol. 73, 1101-1114
161. Treusch, S. and Lindquist, S. (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component J. Cell Biol. 197, 369-379
162. Benko, A. L., Vaduva, G., Martin, N. C., and Hopper, A. K. (2000) Competition between a sterol biosynthetic enzyme and tRNA modification in addition to changes in the protein synthesis machinery causes altered nonsense suppression Proc. Natl. Acad. Sci. U.S.A. 97, 61-66 (Pubitemid 30055784)
163. Chernoff, Y. O., Galkin, A. P., Lewitin, E., Chernova, T. A., Newnam, G. P., and Belenkiy, S. M. (2000) Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein Mol. Microbiol. 35, 865-876 (Pubitemid 30107537)
164. Santoso, A., Chien, P., Osherovich, L. Z., and Weissman, J. S. (2000) Molecular basis of a yeast prion species barrier Cell 100, 277-288 (Pubitemid 30064915)
165. 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 (Pubitemid 30072602)
166. Nakayashiki, T., Ebihara, K., Bannai, H., and Nakamura, Y. (2001) Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state Mol. Cell 7, 1121-1130 (Pubitemid 32607347)
167. Edskes, H. K. and Wickner, R. B. (2002) 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) 16384-16391 (Pubitemid 35470983)
168. Baudin-Baillieu, A., Fernandez-Bellot, E., Reine, F., Coissac, E., and Cullin, C. (2003) Conservation of the prion properties of Ure2p through evolution Mol. Biol. Cell 14, 3449-3458 (Pubitemid 37013140)
169. Safadi, R. A., Talarek, N., Jacques, N., and Aigle, M. (2011) Yeast prions: Could they be exaptations? The URE2 /[URE3] system in Kluyveromyces lactis FEMS Yeast Res. 11, 151-153
170. Edskes, H. K., Engel, A., McCann, L. M., Brachmann, A., Tsai, H.-F., and Wickner, R. B. (2011) Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved Genetics 188, 81-90
171. Edskes, H. K. and Wickner, R. B. The [URE3] prion in Candida. Eukaryotic Cell 2013, in press.
172. Hoshino, S., Imai, M., Kobayashi, T., Uchida, N., and Katada, T. (1999) The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA J. Biol. Chem. 274, 16677-16680
173. Kiktev, D. A., Patterson, J. C., Muller, S., Bariar, B., Pan, T., and Chernoff, Y. O. (2012) Regulation of the chaperone effects on a yeast prion by the cochaperone Sgt2 Mol. Cell. Biol. 32, 4960-4970
174. Mead, S., Stumpf, M. P., Whitfield, J., Beck, J. A., Poulter, M., Campbell, T., Uphill, J. B., Goldstein, D., Alpers, M., Fisher, E. M., and Collinge, J. (2003) Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics Science 300, 640-643 (Pubitemid 36520588)
175. Collinge, J. and Clarke, A. R. (2007) A general model of prion strains and their pathogenicity Science 318, 930-936 (Pubitemid 350098981)
176. Li, J., Browning, S., Mahal, S. P., Oelschlegel, A. M., and Weissmann, C. (2010) Darwinian evolution of prions in cell culture Science 327, 869-872
177. Bateman, D., Tycko, R., and Wickner, R. B. (2011) Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretin Biophys. J. 101, 2485-2492
178. Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., and Meier, B. H. (2008) Amyloid fibrils of the HET-s(218-279) prion form a β solenoid with a triangular hydrophobic core Science 319, 1523-1526 (Pubitemid 351398180)
179. Shewmaker, F., McGlinchey, R., Thurber, K. R., McPhie, P., Dyda, F., Tycko, R., and Wickner, R. B. (2009) The functional curli amyloid is not based on in-register parallel β-sheet structure J. Biol. Chem. 284, 25065-25076
180. Hu, K.-N., McGlinchey, R., Wickner, R. B., and Tycko, R. (2011) Segmental polymorphism in a functional amyloid Biophys. J. 101, 2242-2250
181. Westermark, G. P. and Westermark, P. (2010) Prion-like aggregates: Infectious agents in human disease Trends Mol. Med. 16, 501-507
182. Junker, M. and Walker, L. C. (2011) Pathogenic protein seeding in Alzheimer's disease and other neurodegenerative disorders Ann. Neurol. 70, 532-540
183. Meriin, A. B., Zhang, X., Alexandrov, I. M., Salnikova, A. B., Ter-Avanesyan, M. D., Chernoff, Y. O., and Sherman, M. Y. (2007) Endocytosis machinery is involved in aggregation of proteins with expanded polyglutamine domains FEBS J. 21, 1915-1925 (Pubitemid 46855636)
184. Tribouillard-Tanvier, D., Dos Reis, S., Gug, F., Voisset, C., Beringue, V., Sabate, R., Kikovska, E., Talarek, N., Bach, S., Huang, C., Desban, N., Saupe, S. J., Supattapone, S., Thuret, J.-Y., Chedin, S., Vilette, D., Galons, H., Sanyal, S., and Blondel, M. (2008) Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs PLoS One 3, e2174
185. Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O., Riekel, C., Grothe, R., and Eisenberg, D. (2005) Structure of the cross-β spine of amyloid-like fibrils Nature 435, 773-778 (Pubitemid 40839722)
186. Eanes, E. D. and Glenner, G. G. (1968) X-ray diffraction studies on amyloid filaments J. Histochem. Cytochem. 16, 673-677
187. Masison, D. C., Kirkland, P. A., and Sharma, D. (2009) Influence of Hsp70s and their regulators on yeast prion propagation Prion 3, 65-73