1,372
Views
19
CrossRef citations to date
0
Altmetric
Profiles and Legacies

[PSI+] turns 50

, &
Pages 318-332 | Received 30 Sep 2015, Accepted 17 Oct 2015, Published online: 21 Dec 2015

REFERENCES

  • Cox BS. [PSI], a cytoplasmic suppressor of super-suppressors in yeast. Heredity 1965; 20:505-21; http://dx.doi.org/10.1038/hdy.1965.65.
  • Ephrussi B, Hottinguer H, Chimenes AM. Action de l'acriflavine sur les levures. I. La mutation“petitie colonie.” Ann Inst Pasteur 1949; 76:351-67.
  • Ephrussi B. Nucleo-cytoplasmic relations in micro-organsims 1953; Claredon Press, Oxford.
  • Aigle M, Lacroute F. Genetical aspects of [URE3], a non-Mendelian, cytoplasmically-inherited mutation in yeast. Mol Gen Genet 1975; 136:327-35; PMID:16095000; http://dx.doi.org/10.1007/BF00341717.
  • Lacroute F. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J Bacteriol 1971; 106:519-22; PMID:5573734.
  • Woods DR, Bevan EA. Studies on the nature of the killer factor produced by Saccharomyces cerevisiae. J Gen Microbiol 1968; 51:115-26; PMID:5653223; http://dx.doi.org/10.1099/00221287-51-1-115.
  • Somers JM, Bevan EA. The inheritance of the killer character in yeast. Genet Res 1969; 13:71-83; PMID:5771662; http://dx.doi.org/10.1017/S0016672300002743.
  • Young CS, Cox BS. Extrachromosomal elements in a super-suppression system of yeast. II. Relations with other extrachromosomal elements. Heredity 1972; 28:189-99; PMID:4555664; http://dx.doi.org/10.1038/hdy.1972.24.
  • Tuite MF, Lund PM, Futcher AB, Dobson MJ, Cox BS, McLaughlin CS. Relationship of the [psi] factor with other plasmids of Saccharomyces cerevisiae. Plasmid 1982; 8:103-11; PMID:6757991; http://dx.doi.org/10.1016/0147-619X(82)90048-8.
  • Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264:566-9; PMID:7909170; http://dx.doi.org/10.1126/science.7909170.
  • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; PMID:6801762; http://dx.doi.org/10.1126/science.6801762.
  • Prusiner SB. Biology and genetics of prions causing neurodegeneration. Annu Rev Genet; 47:601-23; PMID:24274755; http://dx.doi.org/10.1146/annurev-genet-110711-155524.
  • Bueler H, Aguzzi A, Sailer A, Greiner RA, Autenried P, Aguet M, Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73:1339-47; PMID:8100741; http://dx.doi.org/10.1016/0092-8674(93)90360-3.
  • Cox BS, Tuite MF, McLaughlin CS. The psi factor of yeast: a problem in inheritance. Yeast 1988; 4:159-78; PMID:3059716; http://dx.doi.org/10.1002/yea.320040302.
  • Liebman S, Sherman F. Extrachromosomal psi+ determinant suppresses nonsense mutations in yeast. J Bacteriol 1979; 139:1068-71; PMID:225301.
  • Tuite MF, Cox BS, McLaughlin CS. In vitro nonsense suppression in [psi+] and [psi-] cell-free lysates of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 1983; 80:2824-8; PMID:6344070; http://dx.doi.org/10.1073/pnas.80.10.2824.
  • Tuite MF, Cox BS, McLaughlin CS. A ribosome-associated inhibitor of in vitro nonsense suppression in [psi-] strains of yeast. FEBS Lett 1987; 225:205-8; PMID:3319694; http://dx.doi.org/10.1016/0014-5793(87)81158-4.
  • Doel SM, McCready SJ, Nierras CR, Cox BS. The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 1994; 137:659-70; PMID:8088511.
  • 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; 137:671-6; PMID:8088512.
  • Cox B. Cytoplasmic inheritance. Prion-like factors in yeast. Curr Biol 1994; 4:744-8; PMID:7953567; http://dx.doi.org/10.1016/S0960-9822(00)00167-6.
  • Patino MM, Liu JJ, Glover JR, Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 1996; 273:622-6; PMID:8662547; http://dx.doi.org/10.1126/science.273.5275.622.
  • 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; 15:3127-34; PMID:8670813.
  • Novick A, Weiner M. Enzyme induction as an all-or-none phenomenon. Proc Natl Acad Sci U S A 1957; 43:553-66; PMID:16590055; http://dx.doi.org/10.1073/pnas.43.7.553.
  • Holliday R, Pugh JE. DNA modification mechanisms and gene activity during development. Science 1975; 187:226-32; PMID:1111098; http://dx.doi.org/10.1126/science.1111098.
  • Holliday R. The inheritance of epigenetic defects. Science 1987; 238:163-70; PMID:3310230; http://dx.doi.org/10.1126/science.3310230.
  • 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; 24:268-70; PMID:8221937; http://dx.doi.org/10.1007/BF00351802.
  • Ter-Avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, Inge-Vechtomov SG, Smirnov VN. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 1993; 7:683-92; PMID:8469113; http://dx.doi.org/10.1111/j.1365-2958.1993.tb01159.x.
  • Wilson PG, Culbertson MR. SUF12 suppressor protein of yeast. A fusion protein related to the EF-1 family of elongation factors. J Mol Biol 1988; 199:559-73; PMID:3280807; http://dx.doi.org/10.1016/0022-2836(88)90301-4.
  • Kikuchi Y, Shimatake H, Kikuchi A. A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain. EMBO J 1988; 7:1175-82; PMID:2841115.
  • Tuite MF, Mundy CR, Cox BS. Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 1981; 98:691-711; PMID:7037537.
  • Munday CR. The genetics of translation in yeast. DPhil Thesis, University of Oxford 1979.
  • Cox BS, Tuite MF, Mundy CJ. Reversion from suppression to nonsuppression in SUQ5 [psi+] strains of yeast: the classificaion of mutations. Genetics 1980; 95:589-609; PMID:7002720.
  • Cox BS. Allosuppressors in yeast. Genet Res 1977; 30:187-205; http://dx.doi.org/10.1017/S0016672300017584.
  • Chabelskaya S, Kiktev D, Inge-Vechtomov S, Philippe M, Zhouravleva G. Nonsense mutations in the essential gene SUP35 of Saccharomyces cerevisiae are non-lethal. Mol Genet Genomics 2004; 272:297-307; PMID:15349771; http://dx.doi.org/10.1007/s00438-004-1053-1.
  • Eaglestone SS, Ruddock LW, Cox BS, Tuite MF. 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 2000; 97:240-4; PMID:10618402; http://dx.doi.org/10.1073/pnas.97.1.240.
  • 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; 268:880-4; PMID:7754373; http://dx.doi.org/10.1126/science.7754373.
  • Young CSH, Cox BS. Extrachromosomal elements in a super-suppression system of yeast. I. A nuclear gene controlling the inheritance of the extrachromosomal elements. Heredity 1971; 26:413-22; http://dx.doi.org/10.1038/hdy.1971.52.
  • Dai H, Tsay SH, Lund PM, Cox BS. Transformation of psi- Saccharomyces cerevisiae to psi+ with DNA co-purified with 3 micron circles. Curr Genet 1986; 11:79-82; PMID:3329046; http://dx.doi.org/10.1007/BF00389429.
  • Tuite MF. Genetics of nonsense supressors in yeast. PhD thesis 1978; University of Oxford.
  • 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; 89:811-9; PMID:9182769; http://dx.doi.org/10.1016/S0092-8674(00)80264-0.
  • Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. In vitro propagation of the prion-like state of yeast Sup35 protein. Science 1997; 277:381-3; PMID:9219697; http://dx.doi.org/10.1126/science.277.5324.381.
  • King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004; 428:319-23; PMID:15029195; http://dx.doi.org/10.1038/nature02391.
  • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variations in an infectious protein determine prion strain differences. Nature 2004; 428:323-8; PMID:15029196; http://dx.doi.org/10.1038/nature02392.
  • Cox BS, Ness F, Tuite MF. Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast. Genetics 2003; 165:23-33; PMID:14504215.
  • Ferreira PC, Ness F, Edwards SR, Cox BS, Tuite MF. The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol 2001; 40:1357-69; PMID:11442834; http://dx.doi.org/10.1046/j.1365-2958.2001.02478.x.
  • Jung G, Masison DC. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol 2001; 43:7-10; PMID:11375656; http://dx.doi.org/10.1007/s002840010251.
  • Winkler J, Tyedmers J, Bukau B, Mogk A. Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 2012; 179:152-60; PMID:22580344; http://dx.doi.org/10.1016/j.jsb.2012.05.002.
  • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146-58; PMID:19345193; http://dx.doi.org/10.1016/j.cell.2009.02.044.
  • Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN+]. Cell 2001; 106:171-82; PMID:11511345; http://dx.doi.org/10.1016/S0092-8674(01)00427-5.
  • Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell 2001; 106:183-94; PMID:11511346; http://dx.doi.org/10.1016/S0092-8674(01)00440-8.
  • Cascarina SM, Ross ED. Yeast prions and human prion-like proteins: sequence features and prediction methods. Cell Mol Life Sci 2014; 71:2047-63; PMID:24390581; http://dx.doi.org/10.1007/s00018-013-1543-6.
  • Soto C. Prion hypothesis: the end of the controversy? Trends Biochem Sci 2011; 36:151-8; PMID:21130657; http://dx.doi.org/10.1016/j.tibs.2010.11.001.
  • Cox BS. A recessive lethal super-suppressor mutation in yeast and other psi phenomena. Heredity 1971; 26:211-32; PMID:5286385; http://dx.doi.org/10.1038/hdy.1971.28.
  • McGlinchey RP, Kryndushkin D, Wickner RB. Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 2011; 108:5337-41; PMID:21402947; http://dx.doi.org/10.1073/pnas.1102762108.
  • Halfmann R, Alberti S, Krishnan R, Lyle N, O'Donnell CW, King OD, Berger B, Pappu RV, Lindquist S. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 2011; 43:72-84; PMID:21726811; http://dx.doi.org/10.1016/j.molcel.2011.05.013.
  • MacLea KS, Paul KR, Ben-Musa Z, Waechter A, Shattuck JE, Gruca M, Ross ED. Distinct amino acid compositional requirements for formation and maintenance of the [PSI+] prion in yeast. Mol Cell Biol 2015; 35:899-911; PMID:25547291; http://dx.doi.org/10.1128/MCB.01020-14.
  • Toombs JA, McCarty BR, Ross ED. Compositional determinants of prion formation in yeast. Mol Cell Biol 2010; 30:319-32; PMID:19884345; http://dx.doi.org/10.1128/MCB.01140-09.
  • Parham SN, Resende CG, Tuite MF. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J 2001; 20:2111-9; PMID:11331577; http://dx.doi.org/10.1093/emboj/20.9.2111.
  • 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; 172:827-35; PMID:16272413; http://dx.doi.org/10.1534/genetics.105.048660.
  • Osherovich LZ, Cox BS, Tuite MF, Weissman JS. Dissection and design of yeast prions. PLoS Biol 2004; 2:E86; PMID:15045026; http://dx.doi.org/10.1371/journal.pbio.0020086.
  • Summers DW, Cyr DM. Use of yeast as a system to study amyloid toxicity. Methods 2011; 53:226-31; PMID:21115125; http://dx.doi.org/10.1016/j.ymeth.2010.11.007.
  • Tenreiro S, Munder MC, Alberti S, Outeiro TF. Harnessing the power of yeast to unravel the molecular basis of neurodegeneration. J Neurochem 2013; 127:438-52; PMID:23600759; http://dx.doi.org/10.1111/jnc.12271.
  • Marchante R, Rowe M, Zenthon J, Howard MJ, Tuite MF. Structural definition is important for the propagation of the yeast [PSI+] prion. Mol Cell 2013; 50:675-85; PMID:23746351; http://dx.doi.org/10.1016/j.molcel.2013.05.010.
  • Asante EA, Smidak M, Grimshaw A, Houghton R, Tomlinson A, Jeelani A, Jakubcova T, Hamdan S, Richard-Londt A, Linehan JM, et al. A naturally occurring variant of the human prion protein completely prevents prion disease. Nature 2015; 522:478-81; PMID:26061765; http://dx.doi.org/10.1038/nature14510.
  • Mead S, Whitfield J, Poulter M, Shah P, Uphill J, Campbell T, Al-Dujaily H, Hummerich H, Beck J, Mein CA, et al. A novel protective prion protein variant that colocalizes with kuru exposure. N Engl J Med 2009; 361:2056-65; PMID:19923577; http://dx.doi.org/10.1056/NEJMoa0809716.
  • 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; 93:1241-52; PMID:9657156; http://dx.doi.org/10.1016/S0092-8674(00)81467-1.
  • Cavalli-Sforza LL, Menozzi P, Piazza A. The History and Geography of Human Genes. Princeton University Press, Princeton 1994.
  • Sheppard PM. Natutal Selection and Heredity. Hutchinson, London 1958.
  • Ford EB. Ecological Genetics. Chapman & Hall, London 1964.
  • Lund PM, Cox BS. Reversion analysis of [psi−] mutations in Saccharomyces cerevisiae. Genet Res 1981; 37:173-82; PMID:7021322; http://dx.doi.org/10.1017/S0016672300020140.
  • Cox BS. Psi phenomena in yeast. The Early Days of Yeast Genetics 1993; Cold Spring Harbor Laboratory Press: pp219-40.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.