SUP35

Summary

Gene Symbol: SUP35
Description: translation termination factor GTPase eRF3
Alias: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, translation termination factor GTPase eRF3
Species: Saccharomyces cerevisiae S288c
Products:     SUP35

Top Publications

  1. Masel J, Griswold C. The strength of selection against the yeast prion [PSI+]. Genetics. 2009;181:1057-63 pubmed publisher
    ..If mN(e) > 1, then selection should favor the spread of [PSI(+)] resistance modifiers. In this case, rare conditions where [PSI(+)] is adaptive may permit its persistence in the face of negative selection. ..
  2. Dong J, Castro C, Boyce M, Lang M, Lindquist S. Optical trapping with high forces reveals unexpected behaviors of prion fibrils. Nat Struct Mol Biol. 2010;17:1422-30 pubmed publisher
    ..Thus, our results reveal unusually strong noncovalent intermolecular contacts that maintain fibril integrity even when individual monomers partially unfold and extend fibril length. ..
  3. Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 2008;27:2712-24 pubmed publisher
    Self-templating amyloid forms of Sup35 constitute the yeast prion [PSI(+)]. How the protein-remodelling factor, Hsp104, collaborates with other chaperones to regulate [PSI(+)] inheritance remains poorly delineated...
  4. Tanaka M, Collins S, Toyama B, Weissman J. The physical basis of how prion conformations determine strain phenotypes. Nature. 2006;442:585-9 pubmed
    ..Analysis of three distinct prion conformations of yeast Sup35 (the [PSI+] protein determinant) and their in vivo phenotypes reveals that the Sup35 amyloid causing the strongest ..
  5. Merritt G, Naemi W, Mugnier P, Webb H, Tuite M, von der Haar T. Decoding accuracy in eRF1 mutants and its correlation with pleiotropic quantitative traits in yeast. Nucleic Acids Res. 2010;38:5479-92 pubmed publisher
    ..We reassess current models of stop-codon recognition by eRF1 in the light of these new data. ..
  6. Newnam G, Birchmore J, Chernoff Y. Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol. 2011;408:432-48 pubmed publisher
    Yeast prion [PSI(+)] is a self-perpetuating amyloid of the translational termination factor Sup35. Although [PSI(+)] propagation is modulated by heat shock proteins (Hsps), high temperature was previously reported to have little or no ..
  7. Wilson M, Meaux S, Parker R, van Hoof A. Genetic interactions between [PSI+] and nonstop mRNA decay affect phenotypic variation. Proc Natl Acad Sci U S A. 2005;102:10244-9 pubmed
    ..Such a process would allow periodic sampling of the 3' UTR, which can diverge rapidly, for novel and beneficial protein extensions. ..
  8. Song Y, Wu Y, Jung G, Tutar Y, Eisenberg E, Greene L, et al. Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot Cell. 2005;4:289-97 pubmed
    ..To visualize differences in aggregate size, we constructed a Sup35-green fluorescent protein (GFP) fusion (NGMC) that has normal Sup35p function and can propagate like [PSI+]...
  9. Shewmaker F, Wickner R, Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci U S A. 2006;103:19754-9 pubmed
    ..Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent ..

More Information

Publications70

  1. Kiktev D, Patterson J, Muller S, Bariar B, Pan T, Chernoff Y. Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol. 2012;32:4960-70 pubmed publisher
    ..One region of Sgt2 interacts both with the prion domain of Sup35 and with tail-anchored proteins...
  2. van der Wel P, Lewandowski J, Griffin R. Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry. 2010;49:9457-69 pubmed publisher
    ..These experimental data can provide guidance for future work, both experimental and theoretical, and provide insights into the distinction between fibril growth and crystal formation. ..
  3. Reidy M, Masison D. Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104. Mol Cell Biol. 2010;30:3542-52 pubmed publisher
  4. Ganusova E, Ozolins L, Bhagat S, Newnam G, Wegrzyn R, Sherman M, et al. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol. 2006;26:617-29 pubmed
    ..Here, we demonstrate that the yeast prion protein Sup35 interacts with various proteins of the actin cortical cytoskeleton that are involved in endocytosis...
  5. Gross T, Siepmann A, Sturm D, Windgassen M, Scarcelli J, Seedorf M, et al. The DEAD-box RNA helicase Dbp5 functions in translation termination. Science. 2007;315:646-9 pubmed
    ..Therefore, Dbp5 controls the eRF3-eRF1 interaction and thus eRF3-mediated downstream events. ..
  6. Collins S, Douglass A, Vale R, Weissman J. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2004;2:e321 pubmed
    ..Here we study the polymerization of the amyloidogenic yeast prion protein Sup35. Rapid polymerization occurs in the absence of observable intermediates, and both targeted kinetic and direct ..
  7. Eurwilaichitr L, Graves F, Stansfield I, Tuite M. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol Microbiol. 1999;32:485-96 pubmed
  8. Khoshnevis S, Gross T, Rotte C, Baierlein C, Ficner R, Krebber H. The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep. 2010;11:214-9 pubmed publisher
    ..interacts physically with the translation termination factors eukaryotic release factor 1 (eRF1)/Sup45 and eRF3/Sup35 in Saccharomyces cerevisiae...
  9. Shewmaker F, Kryndushkin D, Chen B, Tycko R, Wickner R. Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration. Biochemistry. 2009;48:5074-82 pubmed publisher
    The [PSI(+)] prion is a self-propagating amyloid of the Sup35 protein, normally a subunit of the translation termination factor, but impaired in this vital function when in the amyloid form...
  10. Kawai Noma S, Ayano S, Pack C, Kinjo M, Yoshida M, Yasuda K, et al. Dynamics of yeast prion aggregates in single living cells. Genes Cells. 2006;11:1085-96 pubmed
    ..Single-cell imaging revealed that the visible foci of yeast prion Sup35 fused with GFP are dispersed throughout the cytoplasm during cell growth, but retain the prion phenotype...
  11. Chernova T, Allen K, Wesoloski L, Shanks J, Chernoff Y, Wilkinson K. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J Biol Chem. 2003;278:52102-15 pubmed
    ..the yeast prion [PSI+], a functionally defective self-perpetuating isoform of the translation termination factor Sup35. Conversely, overexpression of ubiquitin (Ub) increases phenotypic expression and induction of [PSI+] in the wild ..
  12. Mukhopadhyay S, Krishnan R, Lemke E, Lindquist S, Deniz A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A. 2007;104:2649-54 pubmed
    The yeast prion protein Sup35 is a translation termination factor, whose activity is modulated by sequestration into a self-perpetuating amyloid...
  13. McGlinchey R, Kryndushkin D, Wickner R. Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A. 2011;108:5337-41 pubmed publisher
    ..Our findings give a more realistic picture of the impact of the prion change than does focus on "mild" prion variants. ..
  14. Kobayashi T, Funakoshi Y, Hoshino S, Katada T. The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J Biol Chem. 2004;279:45693-700 pubmed
    ..The termination reaction itself is not sufficient, but eRF3 is essential for triggering mRNA decay. Thus, eRF3 is a key mediator that transduces termination signal to mRNA decay. ..
  15. Krzewska J, Tanaka M, Burston S, Melki R. Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J Biol Chem. 2007;282:1679-86 pubmed
    The protein Sup35 has prion properties. Its aggregation is at the origin of the [PSI(+)] trait in Saccharomyces cerevisiae...
  16. Akhmaloka -, Susilowati P, Subandi -, Madayanti F. Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3. Int J Biol Sci. 2008;4:87-95 pubmed
    ..The data suggested that increasing stop codon suppression and decreasing of the binding affinity of eRF1(Y410S) were probably due to the slight modification on the structure of the C-terminal domain. ..
  17. Bailleul P, Newnam G, Steenbergen J, Chernoff Y. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics. 1999;153:81-94 pubmed
    ..Sla1 (Sla1C) specifically interacts with the N-terminal prion-forming domain (Sup35N) of the yeast release factor Sup35 (eRF3) in the two-hybrid system...
  18. Hosoda N, Kobayashi T, Uchida N, Funakoshi Y, Kikuchi Y, Hoshino S, et al. Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. J Biol Chem. 2003;278:38287-91 pubmed
    ..These results indicate that the N-domain of eRF3 mediates mRNA decay by regulating deadenylation in a manner coupled to translation. ..
  19. Higurashi T, Hines J, Sahi C, Aron R, Craig E. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A. 2008;105:16596-601 pubmed publisher
  20. Wu Y, Greene L, Masison D, Eisenberg E. Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division. Proc Natl Acad Sci U S A. 2005;102:12789-94 pubmed
    ..Sup35p-GFP; but then, before the yeast divided, the aggregates began to dissolve, and after approximately 6 h the Sup35-GFP looked identical to the Sup35-GFP in [psi+] cells...
  21. Verges K, Smith M, Toyama B, Weissman J. Strain conformation, primary structure and the propagation of the yeast prion [PSI+]. Nat Struct Mol Biol. 2011;18:493-9 pubmed publisher
    ..by exploiting our ability to create two distinct infectious conformations of the yeast [PSI(+)] prion protein Sup35, termed Sc4 and Sc37...
  22. Pezza J, Langseth S, Raupp Yamamoto R, Doris S, Ulin S, Salomon A, et al. The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype. Mol Biol Cell. 2009;20:1068-80 pubmed publisher
    ..cerevisiae Sup35 protein (Sup35([PSI+])), and the three N(alpha)-acetyltransferases, NatA, NatB, and NatC, which collectively ..
  23. Salnikova A, Kryndushkin D, Smirnov V, Kushnirov V, Ter Avanesyan M. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem. 2005;280:8808-12 pubmed
    ..cerevisiae causes nonsense suppressor phenotype due to a reduced function of the translation termination factor Sup35 (eRF3) polymerized into amyloid fibrils...
  24. Czaplinski K, Ruiz Echevarria M, Paushkin S, Han X, Weng Y, Perlick H, et al. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 1998;12:1665-77 pubmed
  25. Paushkin S, Kushnirov V, Smirnov V, Ter Avanesyan M. Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Mol Cell Biol. 1997;17:2798-805 pubmed
    The SUP45 and SUP35 genes of Saccharomyces cerevisiae encode polypeptide chain release factors eRF1 and eRF3, respectively...
  26. Shoemaker C, Eyler D, Green R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science. 2010;330:369-72 pubmed publisher
  27. Chang H, Lin J, Lee H, Wang H, King C. Strain-specific sequences required for yeast [PSI+] prion propagation. Proc Natl Acad Sci U S A. 2008;105:13345-50 pubmed publisher
    ..VL], have been previously characterized and are amyloid conformers of the yeast translation termination factor Sup35. Here we define specific sequences of the Sup35 protein that are necessary for in vivo propagation of each of ..
  28. Cosson B, Couturier A, Chabelskaya S, Kiktev D, Inge Vechtomov S, Philippe M, et al. Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation. Mol Cell Biol. 2002;22:3301-15 pubmed
    ..exists between eRF3 and Pab1p and showed that Pab1p overexpression enhances the efficiency of termination in SUP35 (eRF3) mutant and [PSI(+)] cells. This effect requires the interaction of Pab1p with eRF3...
  29. Vishveshwara N, Bradley M, Liebman S. Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol. 2009;73:1101-14 pubmed publisher
    ..Sup45-GFPp formed puncta that colocalized with large [PSI(+)] Sup35-RFPp aggregates in cells overexpressing Sup35p, and the frequency of the Sup45-GFPp puncta was reduced by rescuing ..
  30. Bagriantsev S, Liebman S. Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J Biol Chem. 2004;279:51042-8 pubmed
    ..These studies demonstrate the intracellular organization of yeast prions and provide insight into the principles of in vivo amyloid assembly. ..
  31. Osherovich L, Cox B, Tuite M, Weissman J. Dissection and design of yeast prions. PLoS Biol. 2004;2:E86 pubmed
    ..Using this knowledge, we have designed novel artificial prions by fusing the replication element of Sup35p to aggregation-prone sequences from other proteins, including pathogenically expanded polyglutamine. ..
  32. Krishnan R, Lindquist S. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature. 2005;435:765-72 pubmed
    ..Amyloid conformers of Sup35 are the molecular embodiment of the yeast prion known as [PSI], which produces heritable changes in phenotype ..
  33. Hung G, Masison D. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics. 2006;173:611-20 pubmed
  34. Stansfield I, Jones K, Kushnirov V, Dagkesamanskaya A, Poznyakovski A, Paushkin S, et al. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 1995;14:4365-73 pubmed
    ..We show, using the two-hybrid system, that in Saccharomyces cerevisiae Sup45p and the product of the SUP35 gene (Sup35p) interact in vivo...
  35. Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science. 2004;304:1793-7 pubmed
    ..of [PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35. Perplexingly, either excess or insufficient Hsp104 eliminates [PSI+]...
  36. Tessier P, Lindquist S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature. 2007;447:556-61 pubmed
    ..For the yeast prion Sup35, we find that the switch to the prion state is controlled with exquisite specificity by small elements of primary ..
  37. Hara H, Nakayashiki T, Crist C, Nakamura Y. Prion domain interaction responsible for species discrimination in yeast [PSI+] transmission. Genes Cells. 2003;8:925-39 pubmed
    The yeast [PSI+] factor is transmitted by a prion mechanism involving self-propagating Sup35 aggregates. As with mammalian prions, a species barrier prevents prion transmission between yeast species...
  38. Saibil H, Seybert A, Habermann A, Winkler J, Eltsov M, Perkovic M, et al. Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A. 2012;109:14906-11 pubmed publisher
    ..One of the best-characterized prions, [PSI(+)], is governed by a conformational change in the prion domain of Sup35, a translation-termination factor...
  39. Namy O, Galopier A, Martini C, Matsufuji S, Fabret C, Rousset J. Epigenetic control of polyamines by the prion [PSI+]. Nat Cell Biol. 2008;10:1069-75 pubmed publisher
    ..Antizyme is the first protein to be described for which expression of its functional form is stimulated by [PSI+]. ..
  40. Urakov V, Valouev I, Lewitin E, Paushkin S, Kosorukov V, Kushnirov V, et al. Itt1p, a novel protein inhibiting translation termination in Saccharomyces cerevisiae. BMC Mol Biol. 2001;2:9 pubmed
    ..This protein possesses a zinc finger domain characteristic of the TRIAD proteins of higher eukaryotes, and this is a first observation of such protein being involved in translation. ..
  41. Krammer C, Kryndushkin D, Suhre M, Kremmer E, Hofmann A, Pfeifer A, et al. The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A. 2009;106:462-7 pubmed publisher
    ..The fact that the yeast Sup35NM domain can propagate as a prion in neuroblastoma cells strongly argues that cellular mechanisms support prion-like inheritance in the mammalian cytosol. ..
  42. Joseph S, Kirkpatrick M. Effects of the [PSI+] prion on rates of adaptation in yeast. J Evol Biol. 2008;21:773-80 pubmed publisher
    ..A major factor affecting the rate of adaptation was initial fitness in the new environment: lines with low initial fitness evolved faster than lines with high initial fitness. ..
  43. Allen K, Wegrzyn R, Chernova T, Muller S, Newnam G, Winslett P, et al. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics. 2005;169:1227-42 pubmed
    PSI(+)] is a prion isoform of the yeast release factor Sup35. In some assays, the cytosolic chaperones Ssa1 and Ssb1/2 of the Hsp70 family were previously shown to exhibit "pro-[PSI(+)]" and "anti-[PSI(+)]" effects, ..
  44. Helsen C, Glover J. Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem. 2012;287:542-56 pubmed publisher
    ..Using biochemical methods we identified Hsp104 binding sites in the highly charged middle domain of Sup35, the protein determinant of [PSI+]...
  45. Toyama B, Kelly M, Gross J, Weissman J. The structural basis of yeast prion strain variants. Nature. 2007;449:233-7 pubmed
    ..5), of the yeast Sup35 prion...
  46. Ebihara K, Nakamura Y. C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids. RNA. 1999;5:739-50 pubmed
    ..e., probably uncoupled with GTP hydrolysis), whereas aminoacyl-tRNA binding depends on that of EF-Tu/EF-1alpha(i.e., coupled with GTP hydrolysis), which sheds some light on the mechanism of eRF3 function. ..
  47. Ohta S, Kawai Noma S, Kitamura A, Pack C, Kinjo M, Taguchi H. The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy. Biochem Biophys Res Commun. 2013;442:28-32 pubmed publisher
    ..Yeast prion [PSI(+)] is a protein-based heritable element, in which amyloid aggregates of the Sup35 protein are transmitted to daughter cells...
  48. Shkundina I, Kushnirov V, Tuite M, Ter Avanesyan M. The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants. Genetics. 2006;172:827-35 pubmed
    The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein...
  49. Bardill J, True H. Heterologous prion interactions are altered by mutations in the prion protein Rnq1p. J Mol Biol. 2009;388:583-96 pubmed publisher
    ..These data suggest that this region is important in defining the structure of the [RNQ+] strain variants. These data are consistent with a model of [PSI+] induction caused by physical interactions between Rnq1p and Sup35p. ..
  50. Bolger T, Folkmann A, Tran E, Wente S. The mRNA export factor Gle1 and inositol hexakisphosphate regulate distinct stages of translation. Cell. 2008;134:624-33 pubmed publisher
    ..However, Gle1 also independently mediates initiation. Thus, Gle1 is uniquely positioned to coordinate the mRNA export and translation mechanisms. These results directly impact models for perturbation of Gle1 function in pathophysiology. ..
  51. Derkatch I, Bradley M, Liebman S. Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion. Proc Natl Acad Sci U S A. 1998;95:2400-5 pubmed
    ..We also show that SUP45 overexpression counteracts the growth inhibition usually associated with overexpression of SUP35 in [PSI+] strains. We argue that excess Sup45p inhibits [PSI+] seed formation...
  52. Satpute Krishnan P, Serio T. Prion protein remodelling confers an immediate phenotypic switch. Nature. 2005;437:262-5 pubmed
    ..Here, we determine the changes in protein-state that induce phenotypic switching for the yeast prion Sup35/[PSI(+)]...
  53. Baxa U, Keller P, Cheng N, Wall J, Steven A. In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone. Mol Microbiol. 2011;79:523-32 pubmed publisher
  54. Studte P, Zink S, Jablonowski D, Bär C, von der Haar T, Tuite M, et al. tRNA and protein methylase complexes mediate zymocin toxicity in yeast. Mol Microbiol. 2008;69:1266-77 pubmed publisher
    ..b>Sup35, we observe that SUP45 overexpression and sup45 mutants suppress zymocin...
  55. Borchsenius A, Muller S, Newnam G, Inge Vechtomov S, Chernoff Y. Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet. 2006;49:21-9 pubmed
    The yeast prion [PSI(+)] is a self-perpetuating aggregated isoform of the translation termination factor Sup35. [PSI ( + )] propagation is promoted by moderate levels and antagonized by high levels of the chaperone Hsp104...
  56. Nelson R, Sawaya M, Balbirnie M, Madsen A, Riekel C, Grothe R, et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature. 2005;435:773-8 pubmed
    ..For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian ..
  57. Sideri T, Stojanovski K, Tuite M, Grant C. Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast. Proc Natl Acad Sci U S A. 2010;107:6394-9 pubmed publisher
    ..We show that the yeast Tsa1/Tsa2 Prxs colocalize to ribosomes and function to protect the Sup35 translation termination factor against oxidative stress-induced formation of its heritable [PSI(+)] prion ..
  58. Urakov V, Valouev I, Kochneva Pervukhova N, Packeiser A, Vishnevsky A, Glebov O, 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 pubmed
    ..The screen for mutations which are lethal in combination with the SUP35-C allele encoding eRF3C revealed the sup45 mutations which alter the N-terminal domain of eRF1 and increase ..
  59. Choe Y, Ryu Y, Kim H, Seok Y. Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Eukaryot Cell. 2009;8:968-76 pubmed publisher
    ..of [PSI(+)], the cross-seeding model was suggested, in which Rnq1 aggregates act as imperfect templates for Sup35 aggregation...
  60. DISALVO S, Derdowski A, Pezza J, Serio T. Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol. 2011;18:486-92 pubmed publisher
    ..Here we determine the mechanisms by which two mutants of the Saccharomyces cerevisiae Sup35 protein cure the [PSI(+)] prion...
  61. Bagriantsev S, Gracheva E, Richmond J, Liebman S. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell. 2008;19:2433-43 pubmed publisher
    The [PSI(+)] prion is the aggregated self-propagating form of the Sup35 protein from the yeast Saccharomyces cerevisiae...