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Volumn 51, Issue 6, 2004, Pages 1649-1659

The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; SUP35 PROTEIN; UNCLASSIFIED DRUG;

EID: 1642524541     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2003.03955.x     Document Type: Article
Times cited : (69)

References (69)
  • 1
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen, R.A., and Marsh, R.F. (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66: 2096-2101.
    • (1992) J Virol , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 2
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen, R.A., Kocisko, D.A., Raymond, G.J., Nandan, S., Lansbury, P.T., and Caughey, B. (1995) Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375: 698-700.
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3    Nandan, S.4    Lansbury, P.T.5    Caughey, B.6
  • 4
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N., Ozier-Kalogeropoulos, O., Li, G.Y., Labouesse, M., Minvielle-Sebastia, L., and Lacroute, F. (1991) A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7: 609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.Y.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 7
    • 0000540950 scopus 로고    scopus 로고
    • Strain typing studies of scrapie and BSE
    • Baker, H., and Ridley, R.M. (eds). New Jersey: Humana Press
    • Bruce, M. (1996) Strain typing studies of scrapie and BSE. In Methods in Molecular Medicine: Prion Diseases. Baker, H., and Ridley, R.M. (eds). New Jersey: Humana Press, pp 223-236.
    • (1996) Methods in Molecular Medicine: Prion Diseases , pp. 223-236
    • Bruce, M.1
  • 8
    • 0028782015 scopus 로고
    • Transmission of bovine spongiform encephalopathy and scrapie to mice: Strain variation and the species barrier
    • Bruce, M., Chree, A., McConnell, I., Foster, J., Pearson, G., and Fraser, H. (1994) Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Phil Trans R Soc London B Biol Sci 343: 405-411.
    • (1994) Phil Trans R Soc London B Biol Sci , vol.343 , pp. 405-411
    • Bruce, M.1    Chree, A.2    McConnell, I.3    Foster, J.4    Pearson, G.5    Fraser, H.6
  • 9
    • 0030944992 scopus 로고    scopus 로고
    • Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies
    • Caughey, B., Raymond, G.J., Kocisko, D.A., and Lansbury, P.T., Jr (1997) Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J Virol 71: 4107-4110.
    • (1997) J Virol , vol.71 , pp. 4107-4110
    • Caughey, B.1    Raymond, G.J.2    Kocisko, D.A.3    Lansbury Jr., P.T.4
  • 11
    • 0027483882 scopus 로고
    • Multicopy SUP35 gene induces de novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
    • Chernoff, Y.O., Derkach, I.L., and Inge-Vechtomov, S.G. (1993) Multicopy SUP35 gene induces de novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 24: 268-270.
    • (1993) Curr Genet , vol.24 , pp. 268-270
    • Chernoff, Y.O.1    Derkach, I.L.2    Inge-Vechtomov, S.G.3
  • 12
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff, Y.O., Lindquist, S.L., Ono, B., Inge-Vechtomov, S.G., and Liebman, S.W. (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268: 880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 14
    • 0035826236 scopus 로고    scopus 로고
    • Conformational diversity in a yeast prion dictates its seeding specificity
    • Chien, P., and Weissman, J.S. (2001) Conformational diversity in a yeast prion dictates its seeding specificity. Nature 410: 223-227.
    • (2001) Nature , vol.410 , pp. 223-227
    • Chien, P.1    Weissman, J.S.2
  • 15
    • 0042358923 scopus 로고    scopus 로고
    • Generation of prion transmission barriers by mutational control of amyloid conformations
    • Chien, P., DePace, A.H., Collins, S.R., and Weissman, J.S. (2003) Generation of prion transmission barriers by mutational control of amyloid conformations. Nature 424: 948-951.
    • (2003) Nature , vol.424 , pp. 948-951
    • Chien, P.1    DePace, A.H.2    Collins, S.R.3    Weissman, J.S.4
  • 16
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y., and Fasman, G.D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 47: 45-148.
    • (1978) Adv Enzymol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 18
    • 0001301433 scopus 로고
    • A mutant of Saccharomyces cerevisiae defective for nuclear fusion
    • Conde, J., and Fink, G.R. (1976) A mutant of Saccharomyces cerevisiae defective for nuclear fusion. Proc Natl Acad Sci USA 73: 3651-3655.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 3651-3655
    • Conde, J.1    Fink, G.R.2
  • 19
    • 84966138908 scopus 로고
    • [PSI], a cytoplasmic suppressor of super-suppression in yeast
    • Cox, B.S. (1965) [PSI], a cytoplasmic suppressor of super-suppression in yeast. Heredity 20: 505-520.
    • (1965) Heredity , vol.20 , pp. 505-520
    • Cox, B.S.1
  • 20
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace, A.H., and Weissman, J.S. (2002) Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nature Struct Biol 9: 389-396.
    • (2002) Nature Struct Biol , vol.9 , pp. 389-396
    • Depace, A.H.1    Weissman, J.S.2
  • 21
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace, A.H., Santoso, A., Hillner, P., and Weissman, J.S. (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93: 1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 23
    • 0030833388 scopus 로고    scopus 로고
    • Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae
    • 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.
    • (1997) Genetics , vol.147 , pp. 507-519
    • Derkatch, I.L.1    Bradley, M.E.2    Zhou, P.3    Chernoff, Y.O.4    Liebman, S.W.5
  • 27
    • 0028174948 scopus 로고
    • The dominant PNM2 mutation which eliminates the [PSI] factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene
    • Doel, S.M., McCready, S.J., Nierras, C.R., and Cox, B.S. (1994) The dominant PNM2 mutation which eliminates the [PSI] factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137: 659-670.
    • (1994) Genetics , vol.137 , pp. 659-670
    • Doel, S.M.1    McCready, S.J.2    Nierras, C.R.3    Cox, B.S.4
  • 28
    • 0014687562 scopus 로고
    • Enzymology of the pigmented adenine-requiring mutants of Saccharomyces and Schizosaccharomyces
    • Fisher, C.R. (1969) Enzymology of the pigmented adenine-requiring mutants of Saccharomyces and Schizosaccharomyces. Biochim Biophys Acta 178: 380-388.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 380-388
    • Fisher, C.R.1
  • 29
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J.F., and Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol 266: 540-553.
    • (1996) Methods Enzymol , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 31
    • 0014945333 scopus 로고
    • The petite mutation in yeast. Loss of mitochondrial deoxyribonucleic acid during induction of petites with ethidium bromide
    • Goldring, E.S., Grossman, L.I., Krupnick, D., Cryer, D.R., and Marmur, J. (1970) The petite mutation in yeast. Loss of mitochondrial deoxyribonucleic acid during induction of petites with ethidium bromide. J Mol Biol 52: 323-335.
    • (1970) J Mol Biol , vol.52 , pp. 323-335
    • Goldring, E.S.1    Grossman, L.I.2    Krupnick, D.3    Cryer, D.R.4    Marmur, J.5
  • 32
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith, J.S. (1967) Self-replication and scrapie. Nature 215: 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 34
    • 0035853292 scopus 로고    scopus 로고
    • Supporting the structural basis of prion strains: Induction and identification of [PSI] variants
    • King, C.Y. (2001) Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 307: 1247-1260.
    • (2001) J Mol Biol , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 35
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • 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 USA 94: 6618-6622.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wuthrich, K.6
  • 40
    • 0026773782 scopus 로고
    • Gene products that promote mRNA turnover in Saccharomyces cerevisiae
    • Leeds, P., Wood, J.M., Lee, B.S., and Culbertson, M.R. (1992) Gene products that promote mRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol 12: 2165-2177.
    • (1992) Mol Cell Biol , vol.12 , pp. 2165-2177
    • Leeds, P.1    Wood, J.M.2    Lee, B.S.3    Culbertson, M.R.4
  • 41
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu, J.J., and Lindquist, S. (1999) Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400: 573-576.
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 43
    • 0024576527 scopus 로고
    • The beta-sheet to coil transition
    • Mattice, W.L. (1989) The beta-sheet to coil transition. Annu Rev Biophys Chem 18: 93-111.
    • (1989) Annu Rev Biophys Chem , vol.18 , pp. 93-111
    • Mattice, W.L.1
  • 44
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch, M.D., and Weissman, J.S. (2000) A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 97: 11910-11915.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 45
    • 0034964442 scopus 로고    scopus 로고
    • +] 'prions' that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state
    • +] 'prions' that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol Cell 7: 1121-1130.
    • (2001) Mol Cell , vol.7 , pp. 1121-1130
    • Nakayashiki, T.1    Ebihara, K.2    Bannai, H.3    Nakamura, Y.4
  • 47
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6
  • 48
    • 0035341212 scopus 로고    scopus 로고
    • Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • 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.
    • (2001) EMBO J , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 49
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • 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.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 50
  • 51
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz, M.F., Johnson, T., Suzuki, M., and Finch, J.T. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 91: 5355-5358.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 52
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S.B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 53
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S.B. (1991) Molecular biology of prion diseases. Science 252: 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 55
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J.S., and Richardson, D.C. (2002) Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99: 2754-2759.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 56
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • Santoso, A., Chien, P., Osherovich, L.Z., and Weissman, J.S. (2000) Molecular basis of a yeast prion species barrier. Cell 100: 277-288.
    • (2000) Cell , vol.100 , pp. 277-288
    • Santoso, A.1    Chien, P.2    Osherovich, L.Z.3    Weissman, J.S.4
  • 57
  • 60
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer, N., and Lindquist, S. (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5: 163-172.
    • (2000) Mol Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 61
    • 0029165882 scopus 로고
    • The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae
    • Stansfield, I., Jones, K.M., Kushnirov, V.V., Dagkesamanskaya, A.R., Poznyakovski, A.I., Paushkin, S.V., et al. (1995) The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14: 4365-4373.
    • (1995) EMBO J , vol.14 , pp. 4365-4373
    • Stansfield, I.1    Jones, K.M.2    Kushnirov, V.V.3    Dagkesamanskaya, A.R.4    Poznyakovski, A.I.5    Paushkin, S.V.6
  • 65
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain, S.M., and Lindquist, S. (2002) Prions as protein-based genetic elements. Annu Rev Microbiol 56: 703-741.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 66
    • 0035890264 scopus 로고    scopus 로고
    • Strains of [PSI+] are distinguished by their efficiencies of prion-mediated conformational conversion
    • Uptain, S.M., Sawicki, G.J., Caughey, B., and Lindquist, S. (2001) Strains of [PSI+] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J 20: 6236-6245.
    • (2001) EMBO J , vol.20 , pp. 6236-6245
    • Uptain, S.M.1    Sawicki, G.J.2    Caughey, B.3    Lindquist, S.4
  • 67
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R.B. (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264: 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 69
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva, G., Frolova, L., Le Goff, X., Le Guellec, R., Inge-Vechtomov, S., Kisselev, L., and Philippe, M. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14: 4065-4072.
    • (1995) EMBO J , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1    Frolova, L.2    Le Goff, X.3    Le Guellec, R.4    Inge-Vechtomov, S.5    Kisselev, L.6    Philippe, M.7


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