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Volumn 435, Issue 7043, 2005, Pages 765-772

Structural insights into a yeast prion illuminate nucleation and strain diversity

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DISEASES; NUCLEATION; PROBLEM SOLVING; PROTEINS;

EID: 20444474976     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03679     Document Type: Article
Times cited : (424)

References (51)
  • 2
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien, P., Weissman, J. S. & DePace, A. H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73, 617-656 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    Depace, A.H.3
  • 3
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • doi:10.1038/nrg1616 (in the press)
    • Shorter, J. & Lindquist, S. Prions as adaptive conduits of memory and inheritance. Nature Rev. Genet. doi:10.1038/nrg1616 (in the press).
    • Nature Rev. Genet.
    • Shorter, J.1    Lindquist, S.2
  • 4
    • 0033913783 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?
    • Caughey, B. Transmissible spongiform encephalopathies, amyloidoses and yeast prions: common threads? Nature Med. 6, 751-754 (2000).
    • (2000) Nature Med. , vol.6 , pp. 751-754
    • Caughey, B.1
  • 6
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain, S. M. & Lindquist, S. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56, 703-741 (2002).
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 7
    • 0346186101 scopus 로고    scopus 로고
    • A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in Aplysia
    • Si, K. et al. A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in Aplysia. Cell 115, 893-904 (2003).
    • (2003) Cell , vol.115 , pp. 893-904
    • Si, K.1
  • 8
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the Aplysia CPEB has prion-like properties
    • Si, K., Lindquist, S. & Kandel, E. R. A neuronal isoform of the Aplysia CPEB has prion-like properties. Cell 115, 879-891 (2003).
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 9
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 10
    • 0034760879 scopus 로고    scopus 로고
    • Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae
    • Jensen, M. A., True, H. L., Chernoff, Y. O. & Lindquist, S. Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae. Genetics 159, 527-535 (2001).
    • (2001) Genetics , vol.159 , pp. 527-535
    • Jensen, M.A.1    True, H.L.2    Chernoff, Y.O.3    Lindquist, S.4
  • 11
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • Eaglestone, S. S., Cox, B. S. & Tuite, M. F. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18, 1974-1981 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 12
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True, H. L. & Lindquist, S. L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477-483 (2000).
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 13
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • True, H. L., Berlin, I. & Lindquist, S. L. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431, 184-187 (2004).
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 14
    • 0025521302 scopus 로고
    • Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae
    • Kushnirov, V. V. et al. Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae. Yeast 6, 461-472 (1990).
    • (1990) Yeast , vol.6 , pp. 461-472
    • Kushnirov, V.V.1
  • 15
    • 0027513128 scopus 로고
    • Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein
    • Ter-Avanesyan, M. D. et al. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683-692 (1993).
    • (1993) Mol. Microbiol. , vol.7 , pp. 683-692
    • Ter-Avanesyan, M.D.1
  • 16
    • 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. & Inge-Vechtomov, S. G. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24, 268-270 (1993).
    • (1993) Curr. Genet. , vol.24 , pp. 268-270
    • Chernoff, Y.O.1    Derkach, I.L.2    Inge-Vechtomov, S.G.3
  • 17
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover, J. R. et al. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89, 811-819 (1997).
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1
  • 18
    • 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. & 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 (suppl. 4), 16446-16453 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.SUPPL. 4 , pp. 16446-16453
    • Liu, J.J.1    Sondheimer, N.2    Lindquist, S.L.3
  • 19
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li, L. & Lindquist, S. Creating a protein-based element of inheritance. Science 287, 661-664 (2000).
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.2
  • 20
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio, T. R. et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317-1321 (2000).
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1
  • 21
    • 0035814918 scopus 로고    scopus 로고
    • Bidirectional amyloid fiber growth for a yeast prion determinant
    • Scheibel, T., Kowal, A. S., Bloom, J. D. & Lindquist, S. L. Bidirectional amyloid fiber growth for a yeast prion determinant. Curr. Biol. 11, 366-369 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 366-369
    • Scheibel, T.1    Kowal, A.S.2    Bloom, J.D.3    Lindquist, S.L.4
  • 22
    • 1442330505 scopus 로고    scopus 로고
    • The elongation of yeast prion fibers involves separable steps of association and conversion
    • Scheibel, T., Bloom, J. & Lindquist, S. L. The elongation of yeast prion fibers involves separable steps of association and conversion. Proc. Natl Acad. Sci. USA 101, 2287-2292 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2287-2292
    • Scheibel, T.1    Bloom, J.2    Lindquist, S.L.3
  • 23
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter, J. & Lindquist, S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304, 1793-1797 (2004).
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 24
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S. R., Douglass, A., Vale, R. D. & Weissman, J. S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2, e321 (2004).
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 25
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace, A. H. & Weissman, J. S. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nature Struct. Biol. 9, 389-396 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 389-396
    • DePace, A.H.1    Weissman, J.S.2
  • 26
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King, C. Y. & Diaz-Avalos, R. Protein-only transmission of three yeast prion strains. Nature 428, 319-323 (2004).
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 27
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M., Chien, P., Naber, N., Cooke, R. & Weissman, J. S. Conformational variations in an infectious protein determine prion strain differences. Nature 428, 323-328 (2004).
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 28
    • 1242340413 scopus 로고    scopus 로고
    • β-helix is a likely core structure of yeast prion Sup35 amyloid fibers
    • Kishimoto, A. et al. β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem. Biophys. Res. Commun. 315, 739-745 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 739-745
    • Kishimoto, A.1
  • 29
    • 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. & Weissman, J. S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241-1252 (1998).
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 30
    • 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, 1247-1260 (2001).
    • (2001) J. Mol. Biol. , vol.307 , pp. 1247-1260
    • King, C.Y.1
  • 31
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure
    • Kajava, A. V., Baxa, U., Wickner, R. B. & Steven, A. C. A model for Ure2p prion filaments and other amyloids: the parallel superpleated β-structure. Proc. Natl Acad. Sci. USA 101, 7885-7890 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 32
    • 0034719144 scopus 로고    scopus 로고
    • The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein
    • Kamen, D. E., Griko, Y. & Woody, R. W. The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein. Biochemistry 39, 15932-15943 (2000).
    • (2000) Biochemistry , vol.39 , pp. 15932-15943
    • Kamen, D.E.1    Griko, Y.2    Woody, R.W.3
  • 33
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • Santoso, A., Chien, P., Osherovich, L. Z. & Weissman, J. S. Molecular basis of a yeast prion species barrier. Cell 100, 277-288 (2000).
    • (2000) Cell , vol.100 , pp. 277-288
    • Santoso, A.1    Chien, P.2    Osherovich, L.Z.3    Weissman, J.S.4
  • 34
    • 0042358923 scopus 로고    scopus 로고
    • Generation of prion transmission barriers by mutational control of amyloid conformations
    • Chien, P., DePace, A. H., Collins, S. R. & Weissman, J. S. Generation of prion transmission barriers by mutational control of amyloid conformations. Nature 424, 948-951 (2003).
    • (2003) Nature , vol.424 , pp. 948-951
    • Chien, P.1    DePace, A.H.2    Collins, S.R.3    Weissman, J.S.4
  • 36
    • 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. et al. 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, 12934-12939 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12934-12939
    • Derkatch, I.L.1
  • 37
    • 0034964442 scopus 로고    scopus 로고
    • Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state
    • Nakayashiki, T., Ebihara, K., Bannai, H. & Nakamura, Y. Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol. Cell 7, 1121-1130 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1121-1130
    • Nakayashiki, T.1    Ebihara, K.2    Bannai, H.3    Nakamura, Y.4
  • 38
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu, J. J. & Lindquist, S. Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400, 573-576 (1999).
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 39
    • 0035341212 scopus 로고    scopus 로고
    • Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • Parham, S. N., Resende, C. G. & Tuite, M. F. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20, 2111-2119 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 41
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • Balbirnie, M., Grothe, R. & Eisenberg, D. S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc. Natl Acad. Sci. USA 98, 2375-2380 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 42
    • 1642524541 scopus 로고    scopus 로고
    • The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions
    • Bradley, M. E. & Liebman, S. W. The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions. Mol. Miaobiol. 51, 1649-1659 (2004).
    • (2004) Mol. Miaobiol. , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 43
    • 2942748436 scopus 로고    scopus 로고
    • Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin
    • Eakin, C. M., Attenello, F. J., Morgan, C. J. & Miranker, A. D. Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin. Biochemistry 43, 7808-7815 (2004).
    • (2004) Biochemistry , vol.43 , pp. 7808-7815
    • Eakin, C.M.1    Attenello, F.J.2    Morgan, C.J.3    Miranker, A.D.4
  • 44
    • 4444346811 scopus 로고    scopus 로고
    • Kinetic control of dimer structure formation in amyloid fibrillogenesis
    • Hwang, W., Zhang, S., Kamm, R. D. & Karplus, M. Kinetic control of dimer structure formation in amyloid fibrillogenesis. Proc. Natl Acad. Sci. USA 101, 12916-12921 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12916-12921
    • Hwang, W.1    Zhang, S.2    Kamm, R.D.3    Karplus, M.4
  • 45
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • Lee, S. & Eisenberg, D. Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process. Nature Struct. Biol. 10, 725-730 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 46
    • 0034725656 scopus 로고    scopus 로고
    • A conformation change in the carboxyl terminus of Alzheimer's Aβ (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis
    • Garzon-Rodriguez, W. et al. A conformation change in the carboxyl terminus of Alzheimer's Aβ (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis. J. Biol. Chem. 275, 22645-22649 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 22645-22649
    • Garzon-Rodriguez, W.1
  • 47
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S. & Mandelkow, E. Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41, 14885-14896 (2002).
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 48
    • 0037133587 scopus 로고    scopus 로고
    • Structural studies of the scrapie prion protein by electron crystallography
    • Wille, H. et al. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl Acad. Sci. USA 99, 3563-3568 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3563-3568
    • Wille, H.1
  • 49
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts, C., Wille, H., Prusiner, S. B. & Cohen, F. E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl Acad. Sci. USA 101, 8342-8347 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 50
    • 0031720905 scopus 로고    scopus 로고
    • Sc molecules with different conformations
    • Sc molecules with different conformations. Nature Med. 4, 1157-1165 (1998).
    • (1998) Nature Med. , vol.4 , pp. 1157-1165
    • Safar, J.1
  • 51
    • 17044435107 scopus 로고    scopus 로고
    • Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins
    • Tanaka, M., Chien, P., Yonekura, K. & Weissman, J. S. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121, 49-62 (2005).
    • (2005) Cell , vol.121 , pp. 49-62
    • Tanaka, M.1    Chien, P.2    Yonekura, K.3    Weissman, J.S.4


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