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Volumn 107, Issue 23, 2010, Pages 10596-10601

Conversion of a yeast prion protein to an infectious form in bacteria

Author keywords

PSI+ inducibility factor; Amyloid; Sup35

Indexed keywords

PRION PROTEIN; PROTEIN SUP35; UNCLASSIFIED DRUG;

EID: 77953782617     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913280107     Document Type: Article
Times cited : (50)

References (46)
  • 1
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian Prion Biology: One Century of Evolving Concepts
    • DOI 10.1016/S0092-8674(03)01031-6
    • Aguzzi A, Polymenidou M (2004) Mammalian prion biology: One century of evolving concepts. Cell 116:313-327. (Pubitemid 38167320)
    • (2004) Cell , vol.116 , Issue.2 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 2
    • 1642322462 scopus 로고    scopus 로고
    • Prions of yeast and filamentous fungi: [URE3+], [PSI+], [PIN+], and [Het-s]
    • ed Prusiner SB (Cold Spring Harbor, NY: Cold Spring Harbor Lab Press)
    • Wickner RB, Liebman SW, Saupe SJ (2004) Prions of yeast and filamentous fungi: [URE3+], [PSI+], [PIN+], and [Het-s]. Prion Biology and Diseases, ed Prusiner SB (Cold Spring Harbor, NY: Cold Spring Harbor Lab Press), pp 305-372.
    • (2004) Prion Biology and Diseases , pp. 305-372
    • Wickner, R.B.1    Liebman, S.W.2    Saupe, S.J.3
  • 3
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • DOI 10.1146/annurev.biochem.72.121801.161837
    • Chien P, Weissman JS, DePace AH (2004) Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 73:617-656. (Pubitemid 39050382)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    Depace, A.H.3
  • 5
    • 0041825135 scopus 로고    scopus 로고
    • Analysis of yeast prion aggregates with amyloid-staining compound in vivo
    • Kimura Y, Koitabashi S, Fujita T (2003) Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct Funct 28:187-193. (Pubitemid 37080957)
    • (2003) Cell Structure and Function , vol.28 , Issue.3 , pp. 187-193
    • Kimura, Y.1    Koitabashi, S.2    Fujita, T.3
  • 6
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain SM, 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
  • 7
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • DOI 10.1038/nrg1616
    • Shorter J, Lindquist S (2005) Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 6:435-450. (Pubitemid 40733889)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 8
  • 10
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN(+)]
    • Derkatch IL, Bradley ME, Hong JY, Liebman SW (2001) Prions affect the appearance of other prions: The story of [PIN(+)]. Cell 106:171-182.
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 11
    • 0035958547 scopus 로고    scopus 로고
    • Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion
    • Osherovich LZ, Weissman JS (2001) Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 106:183-194.
    • (2001) Cell , vol.106 , pp. 183-194
    • Osherovich, L.Z.1    Weissman, J.S.2
  • 12
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • DOI 10.1038/ng.112, PII NG112
    • Du Z, Park KW, Yu H, Fan Q, Li L (2008) Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 40: 460-465. (Pubitemid 351450881)
    • (2008) Nature Genetics , vol.40 , Issue.4 , pp. 460-465
    • Du, Z.1    Park, K.-W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 13
    • 60549101873 scopus 로고    scopus 로고
    • A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen
    • Nemecek J, Nakayashiki T, Wickner RB (2009) A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci USA 106:1892-1896.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1892-1896
    • Nemecek, J.1    Nakayashiki, T.2    Wickner, R.B.3
  • 14
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 15
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW (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
  • 16
    • 31444452768 scopus 로고    scopus 로고
    • The battle of the fold: Chaperones take on prions
    • True HL (2006) The battle of the fold: Chaperones take on prions. Trends Genet 22: 110-117.
    • (2006) Trends Genet , vol.22 , pp. 110-117
    • True, H.L.1
  • 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 JR, et al. (1997) Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89:811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1
  • 18
    • 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 MD, Dagkesamanskaya AR, Kushnirov VV, Smirnov VN (1994) The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae. Genetics 137: 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
  • 19
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li L, Lindquist S (2000) Creating a protein-based element of inheritance. Science 287: 661-664.
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.2
  • 20
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu JJ, 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
  • 21
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV (2003) Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278:49636-49643.
    • (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
  • 22
    • 33749632462 scopus 로고    scopus 로고
    • Analysis of amyloid aggregates using agarose gel electrophoresis
    • Bagriantsev SN, Kushnirov VV, Liebman SW (2006) Analysis of amyloid aggregates using agarose gel electrophoresis. Methods Enzymol 412:33-48.
    • (2006) Methods Enzymol , vol.412 , pp. 33-48
    • Bagriantsev, S.N.1    Kushnirov, V.V.2    Liebman, S.W.3
  • 23
    • 80055112289 scopus 로고    scopus 로고
    • Screening for amyloid aggregation by semidenaturing detergent-agarose gel electrophoresis
    • July 16
    • Halfmann R, Lindquist S (July 16, 2008) Screening for amyloid aggregation by semidenaturing detergent-agarose gel electrophoresis. J Vis Exp, 17: 10.3791/838.
    • (2008) J Vis Exp , vol.17
    • Halfmann, R.1    Lindquist, S.2
  • 25
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer N, Lindquist S (2000) Rnq1: An epigenetic modifier of protein function in yeast. Mol Cell 5:163-172. (Pubitemid 30105445)
    • (2000) Molecular Cell , vol.5 , Issue.1 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 27
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DOI 10.1016/S0092-8674(00)81467-1
    • DePace AH, Santoso A, Hillner P, Weissman JS (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93:1241-1252. (Pubitemid 28307428)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1241-1252
    • Depace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 28
    • 33749632460 scopus 로고    scopus 로고
    • An Efficient Protein Transformation Protocol for Introducing Prions into Yeast
    • DOI 10.1016/S0076-6879(06)12012-1, PII S0076687906120121
    • Tanaka M, Weissman JS (2006) An efficient protein transformation protocol for introducing prions into yeast. Methods Enzymol 412:185-200. (Pubitemid 44548581)
    • (2006) Methods in Enzymology , vol.412 , pp. 185-200
    • Tanaka, M.1    Weissman, J.S.2
  • 29
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • DOI 10.1038/nature02392
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428:323-328. (Pubitemid 38418803)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 30
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428:319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 31
    • 0022777250 scopus 로고
    • High-efficiency transformation of Saccharomyces cerevisiae cells by bacterial minicell protoplast fusion
    • Gyuris J, Duda EG (1986) High-efficiency transformation of Saccharomyces cerevisiae cells by bacterial minicell protoplast fusion. Mol Cell Biol 6:3295-3297.
    • (1986) Mol Cell Biol , vol.6 , pp. 3295-3297
    • Gyuris, J.1    Duda, E.G.2
  • 32
    • 0027483882 scopus 로고
    • Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
    • Chernoff YO, Derkach IL, Inge-Vechtomov SG (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
  • 34
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • Tanaka M, Collins SR, Toyama BH, Weissman JS (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442:585-589. (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 35
    • 58849091748 scopus 로고    scopus 로고
    • The yeast Sup35NM domain propagates as a prion in mammalian cells
    • Krammer C, et al. (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci USA 106:462-467.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 462-467
    • Krammer, C.1
  • 36
    • 0034725747 scopus 로고    scopus 로고
    • Evidence for the prion hypothesis: Induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein
    • Sparrer HE, Santoso A, Szoka FCJ, Jr, Weissman JS, (2000) Evidence for the prion hypothesis: Induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein. Science 289:595-599.
    • (2000) Science , vol.289 , pp. 595-599
    • Sparrer, H.E.1    Santoso, A.2    Szoka Jr., F.C.J.3    Weissman, J.S.4
  • 38
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
    • DOI 10.1371/journal.pone.0001763
    • Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andréasson C, Lindquist S, Bukau B (2007) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 3:e1763. (Pubitemid 351903297)
    • (2008) PLoS ONE , vol.3 , Issue.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andreasson, C.5    Lindquist, S.6    Bukau, B.7
  • 40
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • Ness F, Ferreira P, Cox BS, Tuite MF (2002) Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 22:5593-5605.
    • (2002) Mol Cell Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 42
    • 33846973006 scopus 로고    scopus 로고
    • Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance
    • DOI 10.1371/journal.pbio.0050024
    • Satpute-Krishnan P, Langseth SX, Serio TR (2007) Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol, 10.1371/journal. pbio.0050024. (Pubitemid 46256674)
    • (2007) PLoS Biology , vol.5 , Issue.2 , pp. 251-262
    • Satpute-Krishnan, P.1    Langseth, S.X.2    Serio, T.R.3
  • 44
    • 43249090675 scopus 로고    scopus 로고
    • Prion-prion interactions
    • Derkatch IL, Liebman SW (2007) Prion-prion interactions. Prion 1:161-169.
    • (2007) Prion , vol.1 , pp. 161-169
    • Derkatch, I.L.1    Liebman, S.W.2
  • 45
    • 14744274820 scopus 로고    scopus 로고
    • Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum
    • DOI 10.1111/j.1365-2958.2005.04501.x
    • Doan T, Marquis KA, Rudner DZ (2005) Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum. Mol Microbiol 55:1767-1781. (Pubitemid 40445212)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1767-1781
    • Doan, T.1    Marquis, K.A.2    Rudner, D.Z.3
  • 46
    • 33747056003 scopus 로고    scopus 로고
    • A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for HET-s
    • DOI 10.1016/j.jbiotec.2006.03.006, PII S0168165606001994
    • Boyé-Harnasch M, Cullin C (2006) A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for HET-s. J Biotechnol 125:222-230. (Pubitemid 44209198)
    • (2006) Journal of Biotechnology , vol.125 , Issue.2 , pp. 222-230
    • Boye-Harnasch, M.1    Cullin, C.2


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