Site-specific structural analysis of a yeast prion strain with species-specific seeding activity

References

• Selkoe DJ. Alzheimer's disease. In the beginning. Nature 1991; 354:432 - 433
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363 - 13383
   PubMed Web of Science ®Google Scholar
• Aguzzi A, Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 2004; 116:313 - 327
   PubMed Web of Science ®Google Scholar
• Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264:566 - 569
   PubMed Web of Science ®Google Scholar
• Chien P, Weissman JS, DePace AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004; 73:617 - 656
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6:435 - 450
   PubMed Web of Science ®Google Scholar
• Tuite MF, Cox BS. Propagation of yeast prions. Nat Rev Mol Cell Biol 2003; 4:878 - 890
   PubMed Web of Science ®Google Scholar
• Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annu Rev Microbiol 2002; 56:703 - 741
   PubMed Web of Science ®Google Scholar
• Coustou V, Deleu C, Saupe S, 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 USA 1997; 94:9773 - 9778
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 2007; 5:611 - 618
   PubMed Web of Science ®Google Scholar
• Du Z, Park KW, Yu H, Fan Q, Li L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 2008; 40:460 - 465
   PubMed Web of Science ®Google Scholar
• Brown JC, Lindquist S. A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes Dev 2009; 23:2320 - 2332
   PubMed Web of Science ®Google Scholar
• Nemecek J, Nakayashiki T, Wickner RB. A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci USA 2009; 106:1892 - 1896
   PubMed Web of Science ®Google Scholar
• Patel BK, Gavin-Smyth J, Liebman SW. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 2009; 11:344 - 349
   PubMed Web of Science ®Google Scholar
• Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146 - 158
   PubMed Web of Science ®Google Scholar
• Bradley ME, Edskes HK, Hong JY, Wickner RB, Liebman SW. Interactions among prions and prion “strains” in yeast. Proc Natl Acad Sci USA 2002; 99:16392 - 16399
   PubMed Web of Science ®Google Scholar
• True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184 - 187
   PubMed Web of Science ®Google Scholar
• True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477 - 483
   PubMed Web of Science ®Google Scholar
• Eaglestone SS, Cox BS, Tuite MF. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J 1999; 18:1974 - 1981
   PubMedGoogle Scholar
• Liu JJ, Lindquist S. Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast. Nature 1999; 400:573 - 576
   PubMed Web of Science ®Google Scholar
• Parham SN, Resende CG, Tuite MF. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J 2001; 20:2111 - 2119
   PubMed Web of Science ®Google Scholar
• Vital C, Gray F, Vital A, Parchi P, Capellari S, Petersen RB, et al. Prion encephalopathy with insertion of octapeptide repeats: the number of repeats determines the type of cerebellar deposits. Neuropathol Appl Neurobiol 1998; 24:125 - 130
   Google Scholar
• Ter-Avanesyan MD, Dagkesamanskaya AR, Kushnirov VV, Smirnov VN. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 1994; 137:671 - 676
   PubMed Web of Science ®Google Scholar
• Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variations in an infectious protein determine prion strain differences. Nature 2004; 428:323 - 328
   PubMed Web of Science ®Google Scholar
• Krzewska J, Tanaka M, Burston SG, Melki R. Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J Biol Chem 2007; 282:1679 - 1686
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 2006; 23:425 - 438
   PubMed Web of Science ®Google Scholar
• Bruce ME, McConnell I, Fraser H, Dickinson AG. The disease characteristics of different strains of scrapie in Sinc congenic mouse lines: implications for the nature of the agent and host control of pathogenesis. J Gen Virol 1991; 72:595 - 603
   PubMed Web of Science ®Google Scholar
• Caughey B, Raymond GJ, Bessen RA. Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J Biol Chem 1998; 273:32230 - 32235
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Chernoff YO, Kushnirov VV, Inge-Vechtomov SG, Liebman SW. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 1996; 144:1375 - 1386
   PubMed Web of Science ®Google Scholar
• King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004; 428:319 - 323
   PubMed Web of Science ®Google Scholar
• Kocisko DA, Come JH, Priola SA, Chesebro B, Raymond GJ, Lansbury PT, Caughey B. Cell-free formation of protease-resistant prion protein. Nature 1994; 370:471 - 474
   PubMed Web of Science ®Google Scholar
• Pattison IH, Jones KM. Modification of a strain of mouse-adapted scrapie by passage through rats. Res Vet Sci 1968; 9:408 - 410
   PubMed Web of Science ®Google Scholar
• Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, et al. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 1998; 4:1157 - 1165
   PubMed Web of Science ®Google Scholar
• Somerville RA, Oberthur RC, Havekost U, MacDonald F, Taylor DM, Dickinson AG. Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J Biol Chem 2002; 277:11084 - 11089
   Google Scholar
• Chernoff YO, Derkach IL, Inge-Vechtomov SG. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 1993; 24:268 - 270
   PubMed Web of Science ®Google Scholar
• Legname G, Nguyen HO, Baskakov IV, Cohen FE, Dearmond SJ, Prusiner SB. Strain-specified characteristics of mouse synthetic prions. Proc Natl Acad Sci USA 2005; 102:2168 - 2173
   PubMed Web of Science ®Google Scholar
• Foo CK, Ohhashi Y, Kelly MJ, Tanaka M, Weissman JS. Radically different amyloid conformations dictate the seeding specificity of a chimeric sup35 prion. J Mol Biol 2011; 408:1 - 8
   PubMed Web of Science ®Google Scholar
• Toyama BH, Kelly MJ, Gross JD, Weissman JS. The structural basis of yeast prion strain variants. Nature 2007; 449:233 - 237
   PubMed Web of Science ®Google Scholar
• Krishnan R, Lindquist SL. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 2005; 435:765 - 772
   PubMed Web of Science ®Google Scholar
• Bruce KL, Chernoff YO. Sequence specificity and fidelity of prion transmission in yeast. Semin Cell Dev Biol 2011;
   PubMed Web of Science ®Google Scholar
• Engel A, Shewmaker F, Edskes HK, Dyda F, Wickner RB. Amyloid of the Candida albicans Ure2p Prion Domain Is Infectious and Has an In-Register Parallel beta-Sheet Structure. Biochemistry 2011; 50:5971 - 5978
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Galkin AP, Lewitin E, Chernova TA, Newnam GP, Belenkiy SM. Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein. Mol Microbiol 2000; 35:865 - 876
   PubMedGoogle Scholar
• Chien P, Weissman JS. Conformational diversity in a yeast prion dictates its seeding specificity. Nature 2001; 410:223 - 227
   PubMed Web of Science ®Google Scholar
• Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24:519 - 550
   PubMed Web of Science ®Google Scholar
• Kushnirov VV, Kochneva-Pervukhova NV, Chechenova MB, Frolova NS, Ter-Avanesyan MD. Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J 2000; 19:324 - 331
   PubMedGoogle Scholar
• Santoso A, Chien P, Osherovich LZ, Weissman JS. Molecular basis of a yeast prion species barrier. Cell 2000; 100:277 - 288
   PubMed Web of Science ®Google Scholar
• Bruce M, Chree A, McConnell I, Foster J, Pearson G, Fraser H. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B Biol Sci 1994; 343:405 - 411
   PubMed Web of Science ®Google Scholar
• Nakayashiki T, Ebihara K, Bannai H, Nakamura Y. Yeast [PSI+] “prions” that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol Cell 2001; 7:1121 - 1130
   Google Scholar
• Prusiner SB, Scott M, Foster D, Pan KM, Groth D, Mirenda C, et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 1990; 63:673 - 686
   PubMed Web of Science ®Google Scholar
• Resende C, Parham SN, Tinsley C, Ferreira P, Duarte JA, Tuite MF. The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism. Microbiology 2002; 148:1049 - 1060
   PubMed Web of Science ®Google Scholar
• Scott M, Foster D, Mirenda C, Serban D, Coufal F, Walchli M, et al. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989; 59:847 - 857
   PubMed Web of Science ®Google Scholar
• Supattapone S, Bosque P, Muramoto T, Wille H, Aagaard C, Peretz D, et al. Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice. Cell 1999; 96:869 - 878
   PubMed Web of Science ®Google Scholar
• Chen B, Newnam GP, Chernoff YO. Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci USA 2007; 104:2791 - 2796
   PubMed Web of Science ®Google Scholar
• Collinge J, Palmer MS, Sidle KC, Hill AF, Gowland I, Meads J, et al. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 1995; 378:779 - 783
   PubMed Web of Science ®Google Scholar
• Vishveshwara N, Liebman SW. Heterologous cross-seeding mimics cross-species prion conversion in a yeast model. BMC Biol 2009; 7:26
   PubMed Web of Science ®Google Scholar
• Chien P, DePace AH, Collins SR, Weissman JS. Generation of prion transmission barriers by mutational control of amyloid conformations. Nature 2003; 424:948 - 951
   PubMed Web of Science ®Google Scholar
• Collinge J, Sidle KC, Meads J, Ironside J, Hill AF. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 1996; 383:685 - 690
   PubMed Web of Science ®Google Scholar
• Hill AF, Desbruslais M, Joiner S, Sidle KCL, Gowland I, Collinge J, et al. The same prion strain causes vCJD and BSE. Nature 1997; 389:448 - 450
   PubMed Web of Science ®Google Scholar
• Peretz D, Williamson RA, Legname G, Matsunaga Y, Vergara J, Burton DR, et al. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 2002; 34:921 - 932
   PubMed Web of Science ®Google Scholar
• Tanaka M, Chien P, Yonekura K, Weissman JS. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 2005; 121:49 - 62
   PubMed Web of Science ®Google Scholar
• Will RG, Ironside JW, Hornlimann B, Zeidler M. Creutzfeldt-Jakob disease. Lancet 1996; 347:65 - 66
   PubMed Web of Science ®Google Scholar
• Dickinson AG, Meikle VM. A comparison of some biological characteristics of the mouse-passaged scrapie agents, 22A and ME7. Genet Res 1969; 13:213 - 225
   PubMedGoogle Scholar
• Tessier PM, Lindquist S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nat Struct Mol Biol 2009; 16:598 - 605
   PubMed Web of Science ®Google Scholar
• Tessier PM, Lindquist S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 2007; 447:556 - 561
   PubMed Web of Science ®Google Scholar
• DePace AH, Santoso A, Hillner P, Weissman JS. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 1998; 93:1241 - 1252
   PubMed Web of Science ®Google Scholar
• Shivaprasad S, Wetzel R. Scanning cysteine mutagenesis analysis of Abeta-(1–40) amyloid fibrils. J Biol Chem 2006; 281:993 - 1000
   PubMed Web of Science ®Google Scholar
• Liu JJ, Sondheimer N, Lindquist SL. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci USA 2002; 99:16446 - 16453
   PubMed Web of Science ®Google Scholar
• Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 1997; 89:811 - 819
   PubMed Web of Science ®Google Scholar
• Chang HY, Lin JY, Lee HC, Wang HL, King CY. Strain-specific sequences required for yeast [PSI+] prion propagation. Proc Natl Acad Sci USA 2008; 105:13345 - 13350
   PubMed Web of Science ®Google Scholar
• Ohhashi Y, Ito K, Toyama BH, Weissman JS, Tanaka M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol 2010; 6:225 - 230
   Google Scholar
• Chen B, Bruce KL, Newnam GP, Gyoneva S, Romanyuk AV, Chernoff YO. Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol 2010; 76:1483 - 1499
   PubMed Web of Science ®Google Scholar
• Kocisko DA, Priola SA, Raymond GJ, Chesebro B, Lansbury PT Jr, Caughey B. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proc Natl Acad Sci USA 1995; 92:3923 - 3927
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Shewmaker F, Kryndushkin D, Nemecek J. Prion variants, species barriers, generation and propagation. J Biol 2009; 8:47
   PubMedGoogle Scholar
• Edskes HK, McCann LM, Hebert AM, Wickner RB. Prion variants and species barriers among Saccharomyces Ure2 proteins. Genetics 2009; 181:1159 - 1167
   Google Scholar
• King CY. Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 2001; 307:1247 - 1260
   PubMed Web of Science ®Google Scholar
• Chernoff YO. Identity determinants of infectious proteins. Proc Natl Acad Sci USA 2008; 105:13191 - 13192
   PubMed Web of Science ®Google Scholar
• Asante EA, Linehan JM, Desbruslais M, Joiner S, Gowland I, Wood AL, et al. BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO J 2002; 21:6358 - 6366
   PubMed Web of Science ®Google Scholar
• Bartz JC, McKenzie DI, Bessen RA, Marsh RF, Aiken JM. Transmissible mink encephalopathy species barrier effect between ferret and mink: PrP gene and protein analysis. J Gen Virol 1994; 75:2947 - 2953
   PubMedGoogle Scholar
• Raymond GJ, Bossers A, Raymond LD, O'Rourke KI, McHolland LE, Bryant PK 3rd, et al. Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease. EMBO J 2000; 19:4425 - 4430
   PubMed Web of Science ®Google Scholar