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Volumn 365, Issue 3, 2007, Pages 773-782

"Prion-proof" for [PIN+]: Infection with In Vitro-made Amyloid Aggregates of Rnq1p-(132-405) Induces [PIN+]

Author keywords

amyloid like; prion; protein only; Rnq1p; PIN+

Indexed keywords

AMINO ACID; AMYLOID; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; POLYGLUTAMINE; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN; RNQ1P PROTEIN;

EID: 33845605514     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.069     Document Type: Article
Times cited : (128)

References (52)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 3
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J.S. Self-replication and scrapie. Nature 215 (1967) 1043-1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 4
    • 0037047086 scopus 로고    scopus 로고
    • Progress toward an ultimate proof of the prion hypothesis
    • Liebman S. Progress toward an ultimate proof of the prion hypothesis. Proc. Natl Acad. Sci. USA 99 (2002) 9098-9100
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9098-9100
    • Liebman, S.1
  • 5
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264 (1994) 566-569
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 6
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: an epigenetic modifier of protein function in yeast
    • Sondheimer N., and Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 5 (2000) 163-172
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 7
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: the story of [PIN(+)]
    • Derkatch I.L., Bradley M.E., Hong J.Y., and Liebman S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106 (2001) 171-182
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 8
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou V., Deleu C., Saupe S., and 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 94 (1997) 9773-9778
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 10
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King C.Y., and Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 428 (2004) 319-323
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 11
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M., Chien P., Naber N., Cooke R., and Weissman J.S. Conformational variations in an infectious protein determine prion strain differences. Nature 428 (2004) 323-328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 12
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: amyloid of Ure2p is infectious
    • Brachmann A., Baxa U., and Wickner R.B. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J. 24 (2005) 3082-3092
    • (2005) EMBO J. , vol.24 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3
  • 13
    • 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. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl Acad. Sci. USA 94 (1997) 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
  • 15
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor K.L., Cheng N., Williams R.W., Steven A.C., and Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283 (1999) 1339-1343
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 16
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: molecular aspects
    • Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24 (1999) 58-63
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 17
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 20
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J., Saa P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 21
    • 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. Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147 (1997) 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
  • 22
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin A.B., Zhang X., He X., Newnam G.P., Chernoff Y.O., and Sherman M.Y. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 157 (2002) 997-1004
    • (2002) J. Cell Biol. , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 23
    • 4444312783 scopus 로고    scopus 로고
    • 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
    • Derkatch I.L., Uptain S.M., Outeiro T.F., Krishnan R., Lindquist S.L., and Liebman S.W. 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 101 (2004) 12934-12939
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12934-12939
    • Derkatch, I.L.1    Uptain, S.M.2    Outeiro, T.F.3    Krishnan, R.4    Lindquist, S.L.5    Liebman, S.W.6
  • 24
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge J., Sidle K.C., Meads J., Ironside J., and Hill A.F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383 (1996) 685-690
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 25
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation
    • Bruce M.E. TSE strain variation. Br. Med. Bull. 66 (2003) 99-108
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 27
    • 0033106024 scopus 로고    scopus 로고
    • The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3
    • Zhou P., Derkatch I.L., Uptain S.M., Patino M.M., Lindquist S., and Liebman S.W. The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3. EMBO J. 18 (1999) 1182-1191
    • (1999) EMBO J. , vol.18 , pp. 1182-1191
    • Zhou, P.1    Derkatch, I.L.2    Uptain, S.M.3    Patino, M.M.4    Lindquist, S.5    Liebman, S.W.6
  • 28
    • 0035853292 scopus 로고    scopus 로고
    • Supporting the structural basis of prion strains: induction and identification of [PSI] variants
    • King C.Y. Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J. Mol. Biol. 307 (2001) 1247-1260
    • (2001) J. Mol. Biol. , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 31
    • 0028200770 scopus 로고
    • The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae
    • Ter-Avanesyan M.D., Dagkesamanskaya A.R., Kushnirov V.V., and Smirnov V.N. The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 137 (1994) 671-676
    • (1994) Genetics , vol.137 , pp. 671-676
    • Ter-Avanesyan, M.D.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 32
    • 0037059016 scopus 로고    scopus 로고
    • Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]
    • Liu J.J., Sondheimer N., and Lindquist S.L. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc. Natl Acad. Sci. USA 99 (2002) 16446-16453
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16446-16453
    • Liu, J.J.1    Sondheimer, N.2    Lindquist, S.L.3
  • 33
    • 1642524541 scopus 로고    scopus 로고
    • The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions
    • Bradley M.E., and Liebman S.W. The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions. Mol. Microbiol. 51 (2004) 1649-1659
    • (2004) Mol. Microbiol. , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 35
    • 10944273371 scopus 로고    scopus 로고
    • Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast
    • Bagriantsev S., and Liebman S.W. Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J. Biol. Chem. 279 (2004) 51042-51048
    • (2004) J. Biol. Chem. , vol.279 , pp. 51042-51048
    • Bagriantsev, S.1    Liebman, S.W.2
  • 36
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 37
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: amyloid growth occurs by monomer addition
    • Collins S.R., Douglass A., Vale R.D., and Weissman J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLOS Biol. 2 (2004) e321
    • (2004) PLOS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 38
    • 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. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl Acad. Sci. USA 91 (1994) 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
  • 39
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway K.A., Harper J.D., and Lansbury P.T. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39 (2000) 2552-2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 40
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R., and Lindquist S.L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435 (2005) 765-772
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 42
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., and Kushnirov V.V. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278 (2003) 49636-49643
    • (2003) J. Biol. Chem. , vol.278 , pp. 49636-49643
    • Kryndushkin, D.S.1    Alexandrov, I.M.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 43
    • 10944222210 scopus 로고    scopus 로고
    • The [URE3] yeast prion results from protein aggregates that differ from amyloid filaments formed in vitro
    • Ripaud L., Maillet L., Immel-Torterotot F., Durand F., and Cullin C. The [URE3] yeast prion results from protein aggregates that differ from amyloid filaments formed in vitro. J. Biol. Chem. 279 (2004) 50962-50968
    • (2004) J. Biol. Chem. , vol.279 , pp. 50962-50968
    • Ripaud, L.1    Maillet, L.2    Immel-Torterotot, F.3    Durand, F.4    Cullin, C.5
  • 44
    • 22044455269 scopus 로고    scopus 로고
    • A toy model for predicting the rate of amyloid formation from unfolded protein
    • Hall D., Hirota N., and Dobson C.M. A toy model for predicting the rate of amyloid formation from unfolded protein. J. Mol. Biol. 351 (2005) 195-205
    • (2005) J. Mol. Biol. , vol.351 , pp. 195-205
    • Hall, D.1    Hirota, N.2    Dobson, C.M.3
  • 45
    • 0019877808 scopus 로고
    • Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume
    • Atha D.H., and Ingham K.C. Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume. J. Biol. Chem. 256 (1981) 12108-12117
    • (1981) J. Biol. Chem. , vol.256 , pp. 12108-12117
    • Atha, D.H.1    Ingham, K.C.2
  • 46
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: sequences, structures and interactions
    • Ross E.D., Minton A., and Wickner R.B. Prion domains: sequences, structures and interactions. Nature Cell Biol. 7 (2005) 1039-1044
    • (2005) Nature Cell Biol. , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 50
    • 0019604156 scopus 로고
    • Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae
    • Tuite M.F., Mundy C.R., and Cox B.S. Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 98 (1981) 691-711
    • (1981) Genetics , vol.98 , pp. 691-711
    • Tuite, M.F.1    Mundy, C.R.2    Cox, B.S.3
  • 51
    • 0038290253 scopus 로고    scopus 로고
    • Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45
    • Bradley M.E., Bagriantsev S., Vishveshwara N., and Liebman S.W. Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45. Yeast 20 (2003) 625-632
    • (2003) Yeast , vol.20 , pp. 625-632
    • Bradley, M.E.1    Bagriantsev, S.2    Vishveshwara, N.3    Liebman, S.W.4
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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