메뉴 건너뛰기




Volumn 8, Issue 6, 2004, Pages 665-671

Amyloidogenic domains, prions and structural inheritance: Rudiments of early life or recent acquisition?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMYLOID; CHAPERONE; HEAT SHOCK PROTEIN 104; PRION PROTEIN;

EID: 8844238368     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.09.002     Document Type: Review
Times cited : (71)

References (53)
  • 1
    • 0000399441 scopus 로고
    • Cytoplasmic inheritance of the organization of the cell cortex in Paramecium aurelia
    • J. Beisson, and T.M. Sonneborn Cytoplasmic inheritance of the organization of the cell cortex in Paramecium aurelia Proc Natl Acad Sci USA 53 1965 275 282
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 275-282
    • Beisson, J.1    Sonneborn, T.M.2
  • 2
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • S.B. Prusiner Prion diseases and the BSE crisis Science 278 1997 245 251
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 3
    • 0029110883 scopus 로고
    • The chemistry of scrapie infection: Implications of the 'ice 9' metaphor
    • P.T. Lansbury Jr., and B. Caughey The chemistry of scrapie infection: implications of the 'ice 9' metaphor Chem Biol 2 1995 1 5
    • (1995) Chem Biol , vol.2 , pp. 1-5
    • Lansbury Jr., P.T.1    Caughey, B.2
  • 4
    • 0028308104 scopus 로고
    • [URE3] as an altered Ure2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • R.B. Wickner [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
  • 5
    • 0035109347 scopus 로고    scopus 로고
    • Mutation processes at the protein level: Is Lamarck back?
    • Y.O. Chernoff Mutation processes at the protein level: is Lamarck back? Mutat Res 488 2001 39 64
    • (2001) Mutat Res , vol.488 , pp. 39-64
    • Chernoff, Y.O.1
  • 6
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • S.M. Uptain, and S. Lindquist Prions as protein-based genetic elements Annu Rev Microbiol 56 2002 703 741
    • (2002) Annu Rev Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 8
    • 5644261460 scopus 로고    scopus 로고
    • Cellular control of prion formation and propagation in yeast
    • G. Telling Horizon Scientific Press
    • Y.O. Chernoff Cellular control of prion formation and propagation in yeast G. Telling Current Perspectives on Prions and Prion Diseases 2004 Horizon Scientific Press 257 303
    • (2004) Current Perspectives on Prions and Prion Diseases , pp. 257-303
    • Chernoff, Y.O.1
  • 10
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: Structural clues for prion propagation
    • B. Kundu, N.R. Maiti, E.M. Jones, K.A. Surewicz, D.L. Vanik, and W.K. Surewicz Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation Proc Natl Acad Sci USA 100 2003 12069 12074
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12069-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 11
    • 1542379868 scopus 로고    scopus 로고
    • Autocatalytic conversion of recombinant prion proteins displays a species barrier
    • I.V. Baskakov Autocatalytic conversion of recombinant prion proteins displays a species barrier J Biol Chem 279 2004 7671 7677
    • (2004) J Biol Chem , vol.279 , pp. 7671-7677
    • Baskakov, I.V.1
  • 12
    • 0037188506 scopus 로고    scopus 로고
    • Amyloid aggregates of the HET-s prion protein are infectious
    • M.L. Maddelein, S. Dos Reis, S. Duvezin-Caubet, B. Coulary-Salin, and S.J. Saupe Amyloid aggregates of the HET-s prion protein are infectious Proc Natl Acad Sci USA 99 2002 7402 7407 This paper demonstrates that the in vitro-produced aggregated form of the Podospora prion protein Het-s can generate a prion state when transfected into the Podospora cells.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7402-7407
    • Maddelein, M.L.1    Dos Reis, S.2    Duvezin-Caubet, S.3    Coulary-Salin, B.4    Saupe, S.J.5
  • 13
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • ••], this paper provides a first direct confirmation that patterns of prion 'variants' are controlled solely by the prion protein itself.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 14
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • ••], this paper provides a first direct confirmation that patterns of prion 'variants' are controlled solely by the prion protein itself.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 16
    • 1642361660 scopus 로고    scopus 로고
    • The ClpB/Hsp104 molecular chaperone - A protein disaggregating machine
    • S. Lee, M.E. Sowa, J.M. Choi, and F.T. Tsai The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine J Struct Biol 146 2004 99 105
    • (2004) J Struct Biol , vol.146 , pp. 99-105
    • Lee, S.1    Sowa, M.E.2    Choi, J.M.3    Tsai, F.T.4
  • 17
    • 0032503963 scopus 로고    scopus 로고
    • Structure and replication of yeast prions
    • V.V. Kushnirov, and M.D. Ter-Avanesyan Structure and replication of yeast prions Cell 94 1998 13 16
    • (1998) Cell , vol.94 , pp. 13-16
    • Kushnirov, V.V.1    Ter-Avanesyan, M.D.2
  • 19
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
    • V. Grimminger, K. Richter, A. Imhof, J. Buchner, and S. Walter The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104 J Biol Chem 279 2004 7378 7383
    • (2004) J Biol Chem , vol.279 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 20
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • F. Ness, P. Ferreira, B.S. Cox, and M.F. Tuite Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast Mol Cell Biol 22 2002 5593 5605 This paper shows that prion-curing agent guanidine-HCl does not prevent Sup35 aggregation per se.
    • (2002) Mol Cell Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 21
    • 1542782213 scopus 로고    scopus 로고
    • +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • +] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104 J Biol Chem 278 2003 49636 49643 This paper describes the new electrophoresis procedure for measurement of the molecular weights of prion polymers in vivo. By using this procedure, the authors demonstrate the difference in average polymer size between the heritable prion 'variants', and show that growth of yeast cells in the presence of guanidine-HCl results in increased polymer size.
    • (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
  • 22
    • 0037162510 scopus 로고    scopus 로고
    • Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
    • G. Jung, G. Jones, and D.C. Masison Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance Proc Natl Acad Sci USA 99 2002 936 941 This paper shows that mutation of Hsp104 inhibits prion curing by guanidine-HCl, confirming the role of Hsp104 inactivation in curing.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 936-941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 23
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • J. Shorter, and S. Lindquist Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers Science 304 2004 1793 1797 First direct in vitro evidence for the dosage-dependent effect of the Hsp104 chaperone on proliferation of the Sup35 amyloid fibers. This work provides a molecular basis for the previously described in vivo effects of Hsp104 on prions.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 24
    • 19344366926 scopus 로고    scopus 로고
    • Dissection and design of yeast prions
    • L.Z. Osherovich, B.S. Cox, M.F. Tuite, and J.S. Weissman Dissection and design of yeast prions PLoS Biol 2 2004 E86 Based on comparison of the structural and functional organization of prion domains of the yeast proteins Sup35 and New1 and on some previously published results from the Sup35 system, this work establishes a concept of the distinct structural modules responsible for amyloid aggregation and prion propagation.
    • (2004) PLoS Biol , vol.2
    • Osherovich, L.Z.1    Cox, B.S.2    Tuite, M.F.3    Weissman, J.S.4
  • 25
    • 0035803490 scopus 로고    scopus 로고
    • Yeast prion protein derivative defective in aggregate shearing and production of new "seeds"
    • A.S. Borchsenius, R.D. Wegrzyn, G.P. Newnam, S.G. Inge-Vechtomov, and Y.O. Chernoff Yeast prion protein derivative defective in aggregate shearing and production of new "seeds" EMBO J 20 2001 6683 6691
    • (2001) EMBO J , vol.20 , pp. 6683-6691
    • Borchsenius, A.S.1    Wegrzyn, R.D.2    Newnam, G.P.3    Inge-Vechtomov, S.G.4    Chernoff, Y.O.5
  • 27
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • A. Aguzzi, and M. Polymenidou Mammalian prion biology: one century of evolving concepts Cell 116 2004 313 327
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 28
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • A.B. Meriin, X. Zhang, X. He, G.P. Newnam, Y.O. Chernoff, and M.Y. Sherman Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1 J Cell Biol 157 2002 997 1004 This work demonstrates that toxicity of a construct, expressing exon 1 of human huntingtin with extended polyQ region in the yeast system, strictly depends on aggregation promoted by the endogenous yeast prion isoform of the protein Rnq1, thus establishing prions as potential susceptibility factors in the other aggregation-related disorders.
    • (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
  • 30
    • 3042675121 scopus 로고    scopus 로고
    • Observation of sequence specificity in the seeding of protein amyloid fibrils
    • M.R. Krebs, L.A. Morozova-Roche, K. Daniel, C.V. Robinson, and C.M. Dobson Observation of sequence specificity in the seeding of protein amyloid fibrils Protein Sci 13 2004 1933 1938 This work shows that efficiency of cross-seeding of amyloid formation by various proteins in vitro depends strongly on the similarity of their sequences. This finding parallels a 'species barrier' described for prion diseases.
    • (2004) Protein Sci , vol.13 , pp. 1933-1938
    • Krebs, M.R.1    Morozova-Roche, L.A.2    Daniel, K.3    Robinson, C.V.4    Dobson, C.M.5
  • 31
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • A. Santoso, P. Chien, L.Z. Osherovich, and J.S. Weissman Molecular basis of a yeast prion species barrier Cell 100 2000 277 288
    • (2000) Cell , vol.100 , pp. 277-288
    • Santoso, A.1    Chien, P.2    Osherovich, L.Z.3    Weissman, J.S.4
  • 36
    • 0034760879 scopus 로고    scopus 로고
    • Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae
    • M.A. Jensen, H.L. True, Y.O. Chernoff, and S. Lindquist Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae Genetics 159 2001 527 535
    • (2001) Genetics , vol.159 , pp. 527-535
    • Jensen, M.A.1    True, H.L.2    Chernoff, Y.O.3    Lindquist, S.4
  • 37
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J Mol Med 81 2003 678 699
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 38
    • 2442553006 scopus 로고    scopus 로고
    • Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case
    • S. Ventura, J. Zurdo, S. Narayanan, M. Parreno, R. Mangues, B. Reif, F. Chiti, E. Giannoni, C.M. Dobson, F.X. Aviles, and L. Serrano Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case Proc Natl Acad Sci USA 101 2004 7258 7263 This paper shows that a short (6 amino acid) sequence of the amyloidogenic protein, transplanted onto the homologous non-amyloidogenic protein, confers to it an ability to form amyloid fibers.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7258-7263
    • Ventura, S.1    Zurdo, J.2    Narayanan, S.3    Parreno, M.4    Mangues, R.5    Reif, B.6    Chiti, F.7    Giannoni, E.8    Dobson, C.M.9    Aviles, F.X.10    Serrano, L.11
  • 39
    • 0242353209 scopus 로고    scopus 로고
    • Architecture of Ure2p prion filaments: The N-terminal domains form a central core fiber
    • U. Baxa, K.L. Taylor, J.S. Wall, M.N. Simon, N. Cheng, R.B. Wickner, and A.C. Steven Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber J Biol Chem 278 2003 43717 43727 This work provides a valuable insight into a structural organization of the amyloid formed by the yeast prion protein Ure2.
    • (2003) J Biol Chem , vol.278 , pp. 43717-43727
    • Baxa, U.1    Taylor, K.L.2    Wall, J.S.3    Simon, M.N.4    Cheng, N.5    Wickner, R.B.6    Steven, A.C.7
  • 40
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated beta-structure
    • A.V. Kajava, U. Baxa, R.B. Wickner, and A.C. Steven A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure Proc Natl Acad Sci USA 101 2004 7885 7890
    • (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
  • 41
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • M.D. Michelitsch, and J.S. Weissman A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions Proc Natl Acad Sci USA 97 2000 11910 11915
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 42
    • 0033532192 scopus 로고    scopus 로고
    • Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2
    • C. Thual, A.A. Komar, L. Bousset, E. Fernandez-Bellot, and C. Cullin Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2 J Biol Chem 274 1999 13666 13674
    • (1999) J Biol Chem , vol.274 , pp. 13666-13674
    • Thual, C.1    Komar, A.A.2    Bousset, L.3    Fernandez-Bellot, E.4    Cullin, C.5
  • 46
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • M. Balbirnie, R. Grothe, and D.S. Eisenberg An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid Proc Natl Acad Sci USA 98 2001 2375 2380
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 47
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • S. Zhang, T. Holmes, C. Lockshin, and A. Rich Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane Proc Natl Acad Sci USA 90 1993 3334 3338
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 48
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • M.F. Perutz, B.J. Pope, D. Owen, E.E. Wanker, and E. Scherzinger Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques Proc Natl Acad Sci USA 99 2002 5596 5600
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 49
    • 0344490335 scopus 로고    scopus 로고
    • Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition
    • T. Scheibel, R. Parthasarathy, G. Sawicki, X.M. Lin, H. Jaeger, and S.L. Lindquist Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition Proc Natl Acad Sci USA 100 2003 4527 4532 This paper describes in vitro self-assembly of nanowires, capable of conducting electricity, by using the derivative of the Sup35 prion domain which was modified to bind gold particles. This introduces a revolutionary engineering tool with potential applications in nanotechnology.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4527-4532
    • Scheibel, T.1    Parthasarathy, R.2    Sawicki, G.3    Lin, X.M.4    Jaeger, H.5    Lindquist, S.L.6
  • 50
    • 1642524541 scopus 로고    scopus 로고
    • +] prions
    • +] prions Mol Microbiol 51 2004 1649 1659 This work defines the minimal region of Sup35 that is required for the faithful maintenance of the 'variant'-specific prion patterns, as the first 137 amino acids of a protein.
    • (2004) Mol Microbiol , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 51
    • 3442889359 scopus 로고    scopus 로고
    • Synthetic mammalian prions
    • G. Legname, I.V. Baskakov, H.O. Nguyen, D. Riesner, F.E. Cohen, S.J. DeArmond, and S.B. Prusiner Synthetic mammalian prions Science 305 2004 673 676 This paper has demonstrated that in vitro generated amyloid fibres of the deletion derivative of PrP cause development of the neurological disease in the transgenic mice expressing the same deletion version of PrP. Moreover, brain extracts of sick mice were capable of infecting other mice with high levels of PrP production.
    • (2004) Science , vol.305 , pp. 673-676
    • Legname, G.1    Baskakov, I.V.2    Nguyen, H.O.3    Riesner, D.4    Cohen, F.E.5    Dearmond, S.J.6    Prusiner, S.B.7
  • 52
    • 4444312783 scopus 로고    scopus 로고
    • +] prion in yeast and aggregation of Sup35 in vitro
    • +] prion in yeast and aggregation of Sup35 in vitro Proc Natl Acad Sci USA 101 2004 12934 12939 This work shows that newly induced aggregates of the prion-forming protein Sup35 co-localize with pre-existing prion aggregates of another QN-rich protein, Rnq1, and that non-QN-rich aggregates do not facilitate Sup35 aggregation.
    • (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
  • 53
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • E.D. Ross, U. Baxa, and R.B. Wickner Scrambled prion domains form prions and amyloid Mol Cell Biol 24 2004 7206 7213 This work shows that five derivatives of the Ure2 PrD, generated by random shuffling of amino acids, retain prion-forming potential in vivo and amyloid-generating potential in vitro.
    • (2004) Mol Cell Biol , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.