메뉴 건너뛰기




Volumn 9, Issue 1, 2013, Pages

Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CHAPERONE; FUNGAL PROTEIN; GLUTAMINE; HEAT SHOCK PROTEIN 104; PRION PROTEIN; PROTEIN PIN4; PROTEIN SIS1; PROTEIN SUP35; UNCLASSIFIED DRUG;

EID: 84873512659     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003236     Document Type: Article
Times cited : (28)

References (98)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB, (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB, (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
  • 3
    • 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
  • 4
    • 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.
    • (2000) Mol Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 5
    • 0029584303 scopus 로고
    • [PSI+] and [URE3] as yeast prions
    • Wickner RB, Masison DC, Edskes HK, (1995) [PSI+] and [URE3] as yeast prions. Yeast 11: 1671-1685.
    • (1995) Yeast , vol.11 , pp. 1671-1685
    • Wickner, R.B.1    Masison, D.C.2    Edskes, H.K.3
  • 6
    • 84859985750 scopus 로고    scopus 로고
    • A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress
    • Suzuki G, Shimazu N, Tanaka M, (2012) A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress. Science 336: 355-359.
    • (2012) Science , vol.336 , pp. 355-359
    • Suzuki, G.1    Shimazu, N.2    Tanaka, M.3
  • 7
    • 80053569315 scopus 로고    scopus 로고
    • Newly identified prions in budding yeast, and their possible functions
    • Crow ET, Li L, (2011) Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22: 452-459.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 452-459
    • Crow, E.T.1    Li, L.2
  • 8
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • 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.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 9
    • 79959882243 scopus 로고    scopus 로고
    • Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins
    • Halfmann R, Alberti S, Krishnan R, Lyle N, O'Donnell CW, et al. (2011) Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 43: 72-84.
    • (2011) Mol Cell , vol.43 , pp. 72-84
    • Halfmann, R.1    Alberti, S.2    Krishnan, R.3    Lyle, N.4    O'Donnell, C.W.5
  • 10
    • 77955629284 scopus 로고    scopus 로고
    • The effects of amino acid composition on yeast prion formation and prion domain interactions
    • Ross ED, Toombs JA, (2010) The effects of amino acid composition on yeast prion formation and prion domain interactions. Prion 4: 60-65.
    • (2010) Prion , vol.4 , pp. 60-65
    • Ross, E.D.1    Toombs, J.A.2
  • 11
    • 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, Kowal AS, Schirmer EC, Patino MM, Liu JJ, 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    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5
  • 12
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King CY, Tittmann P, Gross H, Gebert R, Aebi M, et al. (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci U S A 94: 6618-6622.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5
  • 13
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
    • AG C, AS K, GJ S, JJ M
    • Serio TR, AG C, AS K, GJ S, JJ M, et al. (2000) Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1
  • 14
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition
    • doi:10.1371/journal.pbio.0020321
    • Collins SR, Douglass A, Vale RD, Weissman JS, (2004) Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition. PLoS Biol 2: e321 doi:10.1371/journal.pbio.0020321.
    • (2004) PLoS Biol , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 15
    • 63449110324 scopus 로고    scopus 로고
    • Life cycle of yeast prions: propagation mediated by amyloid fibrils
    • Inoue Y, (2009) Life cycle of yeast prions: propagation mediated by amyloid fibrils. Protein Pept Lett 16: 271-276.
    • (2009) Protein Pept Lett , vol.16 , pp. 271-276
    • Inoue, Y.1
  • 16
    • 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
  • 17
    • 75349113019 scopus 로고    scopus 로고
    • Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation
    • Haslberger T, Bukau B, Mogk A, (2010) Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol 88: 63-75.
    • (2010) Biochem Cell Biol , vol.88 , pp. 63-75
    • Haslberger, T.1    Bukau, B.2    Mogk, A.3
  • 18
    • 0141455115 scopus 로고    scopus 로고
    • Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast
    • Cox B, Ness F, Tuite M, (2003) Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast. Genetics 165: 23-33.
    • (2003) Genetics , vol.165 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 19
    • 0034602804 scopus 로고    scopus 로고
    • Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae
    • Eaglestone SS, Ruddock LW, Cox BS, Tuite MF, (2000) Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 97: 240-244.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 240-244
    • Eaglestone, S.S.1    Ruddock, L.W.2    Cox, B.S.3    Tuite, M.F.4
  • 20
    • 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
  • 21
    • 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 5: e24 doi:10.1371/journal.pbio.0050024.
    • (2007) PLoS Biol , vol.5
    • Satpute-Krishnan, P.1    Langseth, S.X.2    Serio, T.R.3
  • 22
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S, (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 23
    • 40649098449 scopus 로고    scopus 로고
    • Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    • Tessarz P, Mogk A, Bukau B, (2008) Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol 68: 87-97.
    • (2008) Mol Microbiol , vol.68 , pp. 87-97
    • Tessarz, P.1    Mogk, A.2    Bukau, B.3
  • 24
    • 84863642981 scopus 로고    scopus 로고
    • A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI+]
    • Helsen CW, Glover JR, (2012) A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI+]. Prion 6: 234-239.
    • (2012) Prion , vol.6 , pp. 234-239
    • Helsen, C.W.1    Glover, J.R.2
  • 26
    • 33745419772 scopus 로고    scopus 로고
    • N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
    • Hung GC, Masison DC, (2006) N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics 173: 611-620.
    • (2006) Genetics , vol.173 , pp. 611-620
    • Hung, G.C.1    Masison, D.C.2
  • 27
    • 77649207979 scopus 로고    scopus 로고
    • Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI+] prion but not for prion propagation
    • Moosavi B, Wongwigkarn J, Tuite MF, (2010) Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI+] prion but not for prion propagation. Yeast 27: 167-179.
    • (2010) Yeast , vol.27 , pp. 167-179
    • Moosavi, B.1    Wongwigkarn, J.2    Tuite, M.F.3
  • 28
    • 84855274299 scopus 로고    scopus 로고
    • Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104)
    • Helsen CW, Glover JR, (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem 287: 542-556.
    • (2012) J Biol Chem , vol.287 , pp. 542-556
    • Helsen, C.W.1    Glover, J.R.2
  • 29
    • 84866438776 scopus 로고    scopus 로고
    • Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
    • Winkler J, Tyedmers J, Bukau B, Mogk A, (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198: 387-404.
    • (2012) J Cell Biol , vol.198 , pp. 387-404
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 30
    • 67649361913 scopus 로고    scopus 로고
    • Influence of Hsp70s and their regulators on yeast prion propagation
    • Masison DC, Kirkland PA, Sharma D, (2009) Influence of Hsp70s and their regulators on yeast prion propagation. Prion 3: 65-73.
    • (2009) Prion , vol.3 , pp. 65-73
    • Masison, D.C.1    Kirkland, P.A.2    Sharma, D.3
  • 31
    • 39149142505 scopus 로고    scopus 로고
    • Insights into the mechanism of prion propagation
    • Perrett S, Jones GW, (2008) Insights into the mechanism of prion propagation. Curr Opin Struct Biol 18: 52-59.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 52-59
    • Perrett, S.1    Jones, G.W.2
  • 32
    • 67349190990 scopus 로고    scopus 로고
    • Ssa1 overexpression and [PIN+] variants cure [PSI+] by dilution of aggregates
    • Mathur V, Hong JY, Liebman SW, (2009) Ssa1 overexpression and [PIN+] variants cure [PSI+] by dilution of aggregates. J Mol Biol 390: 155-167.
    • (2009) J Mol Biol , vol.390 , pp. 155-167
    • Mathur, V.1    Hong, J.Y.2    Liebman, S.W.3
  • 33
    • 0036096777 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast [PSI+] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
    • Schwimmer C, Masison DC, (2002) Antagonistic interactions between yeast [PSI+] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol Cell Biol 22: 3590-3598.
    • (2002) Mol Cell Biol , vol.22 , pp. 3590-3598
    • Schwimmer, C.1    Masison, D.C.2
  • 34
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • Aron R, Higurashi T, Sahi C, Craig EA, (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. Embo J 26: 3794-3803.
    • (2007) Embo J , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 36
    • 0035873740 scopus 로고    scopus 로고
    • The role of Sis1 in the maintenance of the [RNQ+] prion
    • Sondheimer N LN, Craig EA, Lindquist S, (2001) The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J 20: 2435-2442.
    • (2001) EMBO J , vol.20 , pp. 2435-2442
    • Sondheimer, N.L.N.1    Craig, E.A.2    Lindquist, S.3
  • 37
    • 79952273241 scopus 로고    scopus 로고
    • [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity
    • doi:10.1371/journal.pgen.1001309
    • Hines JK, Li X, Du Z, Higurashi T, Li L, et al. (2011) [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity. PLoS Genet 7: e1001309 doi:10.1371/journal.pgen.1001309.
    • (2011) PLoS Genet , vol.7
    • Hines, J.K.1    Li, X.2    Du, Z.3    Higurashi, T.4    Li, L.5
  • 38
    • 48749104090 scopus 로고    scopus 로고
    • Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition
    • Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW, (2008) Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition. Mol Biol Cell 19: 2433-2443.
    • (2008) Mol Biol Cell , vol.19 , pp. 2433-2443
    • Bagriantsev, S.N.1    Gracheva, E.O.2    Richmond, J.E.3    Liebman, S.W.4
  • 39
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • Tipton KA, Verges KJ, Weissman JS, (2008) In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol Cell 32: 584-591.
    • (2008) Mol Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 40
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler J, Tyedmers J, Bukau B, Mogk A, (2012) Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 179: 152-160.
    • (2012) J Struct Biol , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 41
    • 34250311267 scopus 로고    scopus 로고
    • Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae
    • Kryndushkin D, Wickner RB, (2007) Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae. Mol Biol Cell 18: 2149-2154.
    • (2007) Mol Biol Cell , vol.18 , pp. 2149-2154
    • Kryndushkin, D.1    Wickner, R.B.2
  • 42
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama H, Edskes HK, Wickner RB, (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol 20: 8916-8922.
    • (2000) Mol Cell Biol , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 43
    • 84966138908 scopus 로고
    • [PSI+], a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS, (1965) [PSI+], a cytoplasmic suppressor of super-suppressor in yeast. Heredity 20: 505-521.
    • (1965) Heredity , vol.20 , pp. 505-521
    • Cox, B.S.1
  • 45
    • 0033555530 scopus 로고    scopus 로고
    • The yeast [PSI+] prion: making sense of nonsense
    • Liebman SW, Derkatch IL, (1999) The yeast [PSI+] prion: making sense of nonsense. J Biol Chem 274: 1181-1184.
    • (1999) J Biol Chem , vol.274 , pp. 1181-1184
    • Liebman, S.W.1    Derkatch, I.L.2
  • 46
    • 0035853292 scopus 로고    scopus 로고
    • Supporting the structural basis of prion strains: induction and identification of [PSI+] variants
    • King CY, (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
  • 48
    • 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 IL, Uptain SM, Patino MM, Lindquist S, et al. (1999) The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3. Embo J 18: 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
  • 49
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • 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.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 50
    • 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
  • 51
    • 0030833388 scopus 로고    scopus 로고
    • Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae
    • Derkatch IL, Bradley ME, Zhou P, Chernoff YO, Liebman SW, (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
  • 52
    • 0034595216 scopus 로고    scopus 로고
    • Dependence and independence of [PSI+] and [PIN+]: a two-prion system in yeast?
    • Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, et al. (2000) Dependence and independence of [PSI+] and [PIN+]: a two-prion system in yeast? Embo J 19: 1942-1952.
    • (2000) Embo J , vol.19 , pp. 1942-1952
    • Derkatch, I.L.1    Bradley, M.E.2    Masse, S.V.3    Zadorsky, S.P.4    Polozkov, G.V.5
  • 54
    • 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 IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, et al. (2004) 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 U S A 101: 12934-12939.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12934-12939
    • Derkatch, I.L.1    Uptain, S.M.2    Outeiro, T.F.3    Krishnan, R.4    Lindquist, S.L.5
  • 55
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin AB, Zhang X, He X, Newnam GP, Chernoff YO, et al. (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 157: 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
  • 56
    • 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
  • 57
    • 67650487949 scopus 로고    scopus 로고
    • Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae
    • Choe YJ, Ryu Y, Kim HJ, Seok YJ, (2009) Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Eukaryot Cell 8: 968-976.
    • (2009) Eukaryot Cell , vol.8 , pp. 968-976
    • Choe, Y.J.1    Ryu, Y.2    Kim, H.J.3    Seok, Y.J.4
  • 58
    • 33847291919 scopus 로고    scopus 로고
    • Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM
    • Vitrenko YA, Gracheva EO, Richmond JE, Liebman SW, (2007) Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. J Biol Chem 282: 1779-1787.
    • (2007) J Biol Chem , vol.282 , pp. 1779-1787
    • Vitrenko, Y.A.1    Gracheva, E.O.2    Richmond, J.E.3    Liebman, S.W.4
  • 59
    • 0346100706 scopus 로고    scopus 로고
    • Destabilizing interactions among [PSI+] and [PIN+] yeast prion variants
    • Bradley ME, Liebman SW, (2003) Destabilizing interactions among [PSI+] and [PIN+] yeast prion variants. Genetics 165: 1675-1685.
    • (2003) Genetics , vol.165 , pp. 1675-1685
    • Bradley, M.E.1    Liebman, S.W.2
  • 60
    • 0033574042 scopus 로고    scopus 로고
    • The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • Edskes HK, Gray VT, Wickner RB, (1999) The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci U S A 96: 1498-1503.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1498-1503
    • Edskes, H.K.1    Gray, V.T.2    Wickner, R.B.3
  • 61
    • 43249121694 scopus 로고    scopus 로고
    • A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates
    • Kurahashi H, Ishiwata M, Shibata S, Nakamura Y, (2008) A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol Cell Biol 28: 3313-3323.
    • (2008) Mol Cell Biol , vol.28 , pp. 3313-3323
    • Kurahashi, H.1    Ishiwata, M.2    Shibata, S.3    Nakamura, Y.4
  • 62
    • 79955083629 scopus 로고    scopus 로고
    • [PSI+] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast
    • Kurahashi H, Pack CG, Shibata S, Oishi K, Sako Y, et al. (2011) [PSI+] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast. Genes Cells 16: 576-589.
    • (2011) Genes Cells , vol.16 , pp. 576-589
    • Kurahashi, H.1    Pack, C.G.2    Shibata, S.3    Oishi, K.4    Sako, Y.5
  • 63
    • 0021028478 scopus 로고
    • The presence of a defective LEU2 gene on 2 mu DNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number
    • Erhart E, Hollenberg CP, (1983) The presence of a defective LEU2 gene on 2 mu DNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number. J Bacteriol 156: 625-635.
    • (1983) J Bacteriol , vol.156 , pp. 625-635
    • Erhart, E.1    Hollenberg, C.P.2
  • 64
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino MM, Liu JJ, Glover JR, 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
  • 65
    • 0035179616 scopus 로고    scopus 로고
    • The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI+] and [PIN+]
    • Zhou P, Derkatch IL, Liebman SW, (2001) The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI+] and [PIN+]. Mol Microbiol 39: 37-46.
    • (2001) Mol Microbiol , vol.39 , pp. 37-46
    • Zhou, P.1    Derkatch, I.L.2    Liebman, S.W.3
  • 66
    • 79959924113 scopus 로고    scopus 로고
    • A new colour assay for [URE3] prion in a genetic background used to score for the [PSI+] prion
    • Hong JY, Mathur V, Liebman SW, (2011) A new colour assay for [URE3] prion in a genetic background used to score for the [PSI+] prion. Yeast 28: 555-560.
    • (2011) Yeast , vol.28 , pp. 555-560
    • Hong, J.Y.1    Mathur, V.2    Liebman, S.W.3
  • 67
    • 24644467295 scopus 로고    scopus 로고
    • Prion protein remodelling confers an immediate phenotypic switch
    • Satpute-Krishnan P, Serio TR, (2005) Prion protein remodelling confers an immediate phenotypic switch. Nature 437: 262-265.
    • (2005) Nature , vol.437 , pp. 262-265
    • Satpute-Krishnan, P.1    Serio, T.R.2
  • 68
    • 70350147706 scopus 로고    scopus 로고
    • Sequestration of essential proteins causes prion associated toxicity in yeast
    • Vishveshwara N, Bradley ME, Liebman SW, (2009) Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 73: 1101-1114.
    • (2009) Mol Microbiol , vol.73 , pp. 1101-1114
    • Vishveshwara, N.1    Bradley, M.E.2    Liebman, S.W.3
  • 69
    • 78049408567 scopus 로고    scopus 로고
    • A size threshold limits prion transmission and establishes phenotypic diversity
    • Derdowski A, Sindi SS, Klaips CL, DiSalvo S, Serio TR, (2011) A size threshold limits prion transmission and establishes phenotypic diversity. Science 330: 680-683.
    • (2011) Science , vol.330 , pp. 680-683
    • Derdowski, A.1    Sindi, S.S.2    Klaips, C.L.3    DiSalvo, S.4    Serio, T.R.5
  • 70
    • 69849100344 scopus 로고    scopus 로고
    • Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI+] cells
    • Kawai-Noma S, Pack CG, Tsuji T, Kinjo M, Taguchi H, (2009) Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI+] cells. Genes Cells 14: 1045-1054.
    • (2009) Genes Cells , vol.14 , pp. 1045-1054
    • Kawai-Noma, S.1    Pack, C.G.2    Tsuji, T.3    Kinjo, M.4    Taguchi, H.5
  • 71
    • 34547453664 scopus 로고    scopus 로고
    • Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride
    • Byrne LJ, Cox BS, Cole DJ, Ridout MS, Morgan BJ, et al. (2007) Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride. Proc Natl Acad Sci U S A 104: 11688-11693.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11688-11693
    • Byrne, L.J.1    Cox, B.S.2    Cole, D.J.3    Ridout, M.S.4    Morgan, B.J.5
  • 72
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: lessons from the yeast model
    • Chernoff YO, (2007) Stress and prions: lessons from the yeast model. FEBS Lett 581: 3695-3701.
    • (2007) FEBS Lett , vol.581 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 73
    • 37249063043 scopus 로고    scopus 로고
    • The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion
    • Fan Q, Park KW, Du Z, Morano KA, Li L, (2007) The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. Genetics 177: 1583-1593.
    • (2007) Genetics , vol.177 , pp. 1583-1593
    • Fan, Q.1    Park, K.W.2    Du, Z.3    Morano, K.A.4    Li, L.5
  • 74
    • 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, Andreasson C, et al. (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3: e1763 doi:10.1371/journal.pone.0001763.
    • (2008) PLoS ONE , vol.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andreasson, C.5
  • 75
    • 79953789286 scopus 로고    scopus 로고
    • Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation
    • Disalvo S, Derdowski A, Pezza JA, Serio TR, (2011) Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol 18: 486-492.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 486-492
    • Disalvo, S.1    Derdowski, A.2    Pezza, J.A.3    Serio, T.R.4
  • 77
  • 78
    • 70350217358 scopus 로고    scopus 로고
    • Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus
    • Douglas PM, Summers DW, Ren HY, Cyr DM, (2009) Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell 20: 4162-4173.
    • (2009) Mol Biol Cell , vol.20 , pp. 4162-4173
    • Douglas, P.M.1    Summers, D.W.2    Ren, H.Y.3    Cyr, D.M.4
  • 79
    • 58849102280 scopus 로고    scopus 로고
    • A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae
    • Ishiwata M, Kurahashi H, Nakamura Y, (2009) A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 106: 791-796.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 791-796
    • Ishiwata, M.1    Kurahashi, H.2    Nakamura, Y.3
  • 80
    • 79958193848 scopus 로고    scopus 로고
    • Molecular Chaperone Hsp104 Can Promote Yeast Prion Generation
    • Kryndushkin DS, Engel A, Edskes HK, Wickner RB, (2011) Molecular Chaperone Hsp104 Can Promote Yeast Prion Generation. Genetics 188: 339-348.
    • (2011) Genetics , vol.188 , pp. 339-348
    • Kryndushkin, D.S.1    Engel, A.2    Edskes, H.K.3    Wickner, R.B.4
  • 81
    • 0037058949 scopus 로고    scopus 로고
    • Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein
    • Edskes HK, Wickner RB, (2002) Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc Natl Acad Sci U S A 99 (Suppl 4) (): 16384-16391.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.SUPPL. 4 , pp. 16384-16391
    • Edskes, H.K.1    Wickner, R.B.2
  • 82
    • 0141864665 scopus 로고    scopus 로고
    • The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products
    • Ripaud L, Maillet L, Cullin C, (2003) The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products. Embo J 22: 5251-5259.
    • (2003) Embo J , vol.22 , pp. 5251-5259
    • Ripaud, L.1    Maillet, L.2    Cullin, C.3
  • 83
    • 79955116719 scopus 로고    scopus 로고
    • Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner
    • Inoue Y, Kawai-Noma S, Koike-Takeshita A, Taguchi H, Yoshida M, (2011) Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Genes Cells 16: 545-556.
    • (2011) Genes Cells , vol.16 , pp. 545-556
    • Inoue, Y.1    Kawai-Noma, S.2    Koike-Takeshita, A.3    Taguchi, H.4    Yoshida, M.5
  • 84
    • 83755183712 scopus 로고    scopus 로고
    • Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements
    • Hines JK, Higurashi T, Srinivasan M, Craig EA, (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5: 238-244.
    • (2011) Prion , vol.5 , pp. 238-244
    • Hines, J.K.1    Higurashi, T.2    Srinivasan, M.3    Craig, E.A.4
  • 85
    • 84861455359 scopus 로고    scopus 로고
    • An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component
    • Treusch S, Lindquist S, (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197: 369-379.
    • (2012) J Cell Biol , vol.197 , pp. 369-379
    • Treusch, S.1    Lindquist, S.2
  • 87
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald ML, Lindquist S, (2008) Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 22: 3308-3319.
    • (2008) Genes Dev , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 88
    • 84860594894 scopus 로고    scopus 로고
    • Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast
    • doi:10.1371/journal.pgen.1002634
    • Gong H, Romanova NV, Allen KD, Chandramowlishwaran P, Gokhale K, et al. (2012) Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8: e1002634 doi:10.1371/journal.pgen.1002634.
    • (2012) PLoS Genet , vol.8
    • Gong, H.1    Romanova, N.V.2    Allen, K.D.3    Chandramowlishwaran, P.4    Gokhale, K.5
  • 89
    • 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 MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, et al. (1993) 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) Mol Microbiol , vol.7 , pp. 683-692
    • Ter-Avanesyan, M.D.1    Kushnirov, V.V.2    Dagkesamanskaya, A.R.3    Didichenko, S.A.4    Chernoff, Y.O.5
  • 90
    • 0014945333 scopus 로고
    • The petite mutation in yeast. Loss of mitochondrial deoxyribonucleic acid during induction of petites with ethidium bromide
    • Goldring ES, Grossman LI, Krupnick D, Cryer DR, 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
  • 91
    • 0019604156 scopus 로고
    • Agents that cause a high frequency of genetic change from [PSI+] to [psi-] in Saccharomyces cerevisiae
    • Tuite MF, Mundy CR, Cox BS, (1981) Agents that cause a high frequency of genetic change from [PSI+] to [psi-] in Saccharomyces cerevisiae. Genetics 98: 691-711.
    • (1981) Genetics , vol.98 , pp. 691-711
    • Tuite, M.F.1    Mundy, C.R.2    Cox, B.S.3
  • 92
    • 0003529274 scopus 로고
    • Methods in Yeast Genetics
    • Sherman F, Fink, G. R. & Hicks, J. B., editor, New York: Cold Spring Harbor Lab
    • Sherman F, Fink, G R & Hicks, J B. (1986) Methods in Yeast Genetics;Sherman F, Fink, G. R. & Hicks, J. B., editor. Plainview, New York: Cold Spring Harbor Lab.
    • (1986) Plainview
    • Sherman, F.1    Fink, G.R.2    Hicks, J.B.3
  • 93
    • 0024841745 scopus 로고
    • Yeast galactose permease is related to yeast and mammalian glucose transporters
    • Nehlin JO, Carlberg M, Ronne H, (1989) Yeast galactose permease is related to yeast and mammalian glucose transporters. Gene 85: 313-319.
    • (1989) Gene , vol.85 , pp. 313-319
    • Nehlin, J.O.1    Carlberg, M.2    Ronne, H.3
  • 96
    • 10944273371 scopus 로고    scopus 로고
    • Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast
    • Bagriantsev S, Liebman SW, (2004) Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J Biol Chem 279: 51042-51048.
    • (2004) J Biol Chem , vol.279 , pp. 51042-51048
    • Bagriantsev, S.1    Liebman, S.W.2
  • 97
    • 0033500152 scopus 로고    scopus 로고
    • Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI+] prion
    • Chernoff YO NG, Kumar J, Allen K, Zink AD, (1999) Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI+] prion. Mol Cell Biol 19: 8103-8112.
    • (1999) Mol Cell Biol , vol.19 , pp. 8103-8112
    • Chernoff, Y.O.N.G.1    Kumar, J.2    Allen, K.3    Zink, A.D.4
  • 98
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: amyloid of Ure2p is infectious
    • Brachmann A, Baxa U, Wickner RB, (2005) Prion generation in vitro: amyloid of Ure2p is infectious. Embo J 24: 3082-3092.
    • (2005) Embo J , vol.24 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.