Interdependence of amyloid formation in yeast

References

• Gebbink MF, Claessen D, Bouma B, Dijkhuizen L, Wösten HA. Amyloids—a functional coat for microorganisms. Nat Rev Microbiol 2005; 3:333 - 341
   PubMed Web of Science ®Google Scholar
• Inge-Vechtomov SG, Zhouravleva GA, Chernoff YO. Biological roles of prion domains. Prion 2007; 1:228 - 235
   PubMed Web of Science ®Google Scholar
• Mironova LN, Goginashvili AI, Ter-Avanesyan MD. Biological functions of amyloids: facts and hypotheses. Mol Biol 2008; 42:710 - 719
   Web of Science ®Google Scholar
• Vishnevskaya AB, Kushnirov VV, Ter-Avanesyan MD. Neurodegenerative amyloidoses: yeast model. Mol Biol 2007; 41:346 - 354
   Web of Science ®Google Scholar
• Kushnirov VV, Vishnevskaya AB, Alexandrov IM, Ter-Avanesyan MD. Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 protein. Prion 2007; 1:179 - 184
   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
• Sondheimer N, Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 2000; 5:163 - 172
   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. Nature Genet 2008; 40:460 - 465
   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
• 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
• Patel BK, Gavin-Smyth J, Liebman SW. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nature Cell Biol 2009; 11:344 - 349
   PubMed Web of Science ®Google Scholar
• Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 1996; 15:3127 - 3134
   PubMed Web of Science ®Google Scholar
• Patino MM, Liu JJ, Glover JR, Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 1996; 273:622 - 626
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN+]. Cell 2001; 106:171 - 182
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. 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. Proc Natl Acad Sci USA 2004; 101:12934 - 12939
   PubMed Web of Science ®Google Scholar
• Salnikova AB, Kryndushkin DS, Smirnov VN, Kushnirov VV, Ter-Avanesyan MD. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 2005; 280:8808 - 8812
   PubMed Web of Science ®Google Scholar
• Cha JH. Transcriptional dysregulation in Huntington’s disease. Trends Neurosci 2000; 23:387 - 392
   PubMed Web of Science ®Google Scholar
• Sugars KL, Rubinsztein DC. Transcriptional abnormalities in Huntington disease. Trends Genet 2003; 19:233 - 238
   PubMed Web of Science ®Google Scholar
• Ciechanover A, Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003; 40:427 - 446
   PubMed Web of Science ®Google Scholar
• Sakahira H, Breuer P, Hayer-Hartl MK, Hartl FU. Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci USA 2002; 99:16412 - 16418
   PubMed Web of Science ®Google Scholar
• Meriin AB, Zhang X, He X, Newnam GP, Chernoff YO, Sherman MY. Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 2002; 157:997 - 1004
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Jagadish S, Giorgini F, Muchowski PJ, Lindquist S. A network of protein interactions determines polyglutamine toxicity. Proc Natl Acad Sci USA 2006; 103:11051 - 11056
   PubMed Web of Science ®Google Scholar
• Wang Y, Meriin AB, Costello CE, Sherman MY. Characterization of proteins associated with polyglutamine aggregates. Prion 2007; 1:128 - 135
   PubMed Web of Science ®Google Scholar
• Alexandrov IM, Vishnevskaya AB, Ter-Avanesyan MD, Kushnirov VV. Appearance and propagation of polyglutamine-based amyloids in yeast: Tyrosine residues enable polymer fragmentation. J Biol Chem 2008; 283:15185 - 15192
   PubMed Web of Science ®Google Scholar
• Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 2003; 278:49636 - 49643
   PubMed Web of Science ®Google Scholar
• Vitrenko YA, Gracheva EO, Richmond JR, Liebman SW. Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J Biol Chem 2007; 282:1779 - 1787
   PubMedGoogle Scholar
• Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 1995; 268:880 - 884
   PubMed Web of Science ®Google Scholar
• Gietz RD, Sugino A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 1988; 74:527 - 534
   PubMed Web of Science ®Google Scholar
• Shkundina IS, Kushnirov VV, Tuite MF, Ter-Avanesyan MD. The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants. Genetics 2006; 172:827 - 835
   PubMed Web of Science ®Google Scholar
• Kushnirov VV, Alexandrov IM, Mitkevich OV, Shkundina IS, Ter-Avanesyan MD. Purification and analysis of prion and amyloid aggregates. Methods 2006; 39:50 - 55
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Jagadish S, Muchowski PJ, Lindquist S. Flanking sequences profoundly alter polyglutamine toxicity in yeast. Proc Natl Acad Sci USA 2006; 103:11045 - 11050
   PubMed Web of Science ®Google Scholar
• Valouev IA, Kushnirov VV, Ter-Avanesyan MD. Yeast polypeptide chain release factors eRF1 and eRF3 are involved in cytoskeleton organization and cell cycle regulation. Cell Motyl Cytoskeleton 2002; 52:161 - 173
   PubMed Web of Science ®Google Scholar
• Taneja V, Maddelein ML, Talarek N, Saupe SJ, Liebman SW. A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast. Mol Cell 2007; 27:67 - 77
   PubMed Web of Science ®Google Scholar
• Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, et al. Global analysis of protein expression in yeast. Nature 2003; 425:737 - 741
   PubMed Web of Science ®Google Scholar
• Wang Y, Meriin AB, Zaarur N, Romanova NV, Chernoff YO, Costello E, Sherman MY. Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 2009; 23:451 - 463
   PubMed Web of Science ®Google Scholar
• Vishveshwara N, Bradley ME, Liebman SW. Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 2009; 73:1101 - 1114
   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
• Ruiz-Echevarria MJ, Peltz SW. The RNA binding protein Pub1 modulates the stability of transcripts containing upstream open reading frames. Cell 2000; 101:741 - 751
   PubMed Web of Science ®Google Scholar
• Duttagupta R, Tian B, Wilusz CJ, Khounh DT, Soteropoulos P, Ouyang M, et al. Global analysis of Pub1p targets reveals a coordinate control of gene expression through modulation of binding and stability. Mol Cell Biol 2005; 25:5499 - 5513
   PubMed Web of Science ®Google Scholar
• Buchan JR, Muhlard D, Parker R. P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 2008; 183:441 - 455
   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
• True HL, Berlin I, Lindquist SL. Epigenetic regulation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184 - 187
   PubMed Web of Science ®Google Scholar
• Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell 2008; 19:2433 - 2443
   Google Scholar
• Mitchelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 2000; 97:11910 - 11915
   PubMed Web of Science ®Google Scholar
• Gokhale KC, Newnam GP, Sherman MY, Chernoff YO. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 2005; 280:22809 - 22818
   PubMed Web of Science ®Google Scholar
• Urakov VN, Valouev IA, Kochneva-Pervukhova NV, Packeiser AN, Vishnevsky AY, Glebov OO, et al. N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination. BMC Mol Biol 2006; 7:34 - 46
   PubMedGoogle Scholar