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Volumn 106, Issue 3, 2009, Pages 791-796

A G-protein γ subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae

Author keywords

PIN+ ; PSI+ ; URE3 ; Gpg1; Yeast prion

Indexed keywords

AMYLOID PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; HEAT SHOCK PROTEIN 104; POLYGLUTAMINE; PRION PROTEIN; TRANSLATION TERMINATION FACTOR; TRANSLATION TERMINATION FACTOR SUP35; UNCLASSIFIED DRUG;

EID: 58849102280     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0808383106     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 2142771202 scopus 로고    scopus 로고
    • Early evidence that a protease-resistant protein is an active component of the infectious prion
    • Prusiner SB (2004) Early evidence that a protease-resistant protein is an active component of the infectious prion. Cell 116:S109.
    • (2004) Cell , vol.116
    • Prusiner, S.B.1
  • 2
    • 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
  • 3
    • 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
  • 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
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • 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.
    • (2008) Nat Genet , vol.40 , pp. 460-465
    • Du, Z.1    Park, K.W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 6
    • 84966138908 scopus 로고
    • ψ, a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS (1965) ψ, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 20:505-521.
    • (1965) Heredity , vol.20 , pp. 505-521
    • Cox, B.S.1
  • 8
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva G, et al. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14:4065-4072.
    • (1995) EMBO J , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1
  • 9
  • 10
    • 0029165882 scopus 로고
    • The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae
    • Stansfield I, et al. (1995) The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14:4365-4373.
    • (1995) EMBO J , vol.14 , pp. 4365-4373
    • Stansfield, I.1
  • 11
    • 58849158390 scopus 로고    scopus 로고
    • +], and Ribosome Recycling (Cold Spring Harbor Laboratory Press, New York) pp 173-196.
    • +], and Ribosome Recycling (Cold Spring Harbor Laboratory Press, New York) pp 173-196.
  • 12
    • 0018734423 scopus 로고
    • + determinant suppresses nonsense mutations in yeast
    • + determinant suppresses nonsense mutations in yeast. J Bacteriol 139:1068-1071.
    • (1979) J Bacteriol , vol.139 , pp. 1068-1071
    • Liebman, S.W.1    Sherman, F.2
  • 13
    • 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
  • 14
    • 33947290033 scopus 로고    scopus 로고
    • Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation
    • Kurahashi H, Nakamura Y (2007) Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation. Mol Microbiol 63:1669-1683.
    • (2007) Mol Microbiol , vol.63 , pp. 1669-1683
    • Kurahashi, H.1    Nakamura, Y.2
  • 15
    • 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
  • 16
    • 0035984604 scopus 로고    scopus 로고
    • The Galpha protein Gpa2 controls yeast differentiation by interacting with kelch repeat proteins that mimic Gbeta subunits
    • Harashima T, Heitman J (2002) The Galpha protein Gpa2 controls yeast differentiation by interacting with kelch repeat proteins that mimic Gbeta subunits. Mol Cell 10:163-173.
    • (2002) Mol Cell , vol.10 , pp. 163-173
    • Harashima, T.1    Heitman, J.2
  • 17
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR (1997) G protein mechanisms: Insights from structural analysis. Annu Rev Biochem 66:639-678.
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 18
    • 15244359991 scopus 로고    scopus 로고
    • Except in every detail: Comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Hoffman CS (2005) Except in every detail: Comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Eukaryot Cell 4:495.
    • (2005) Eukaryot Cell , vol.4 , pp. 495
    • Hoffman, C.S.1
  • 22
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • Magasanik B, Kaiser CA (2002) Nitrogen regulation in Saccharomyces cerevisiae. Gene 290:1-18.
    • (2002) Gene , vol.290 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 23
    • 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
  • 24
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin AB, 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
  • 25
    • 20744441099 scopus 로고    scopus 로고
    • Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model
    • Gokhale KC, Newnam GP, Sherman MY, Chernoff YO (2005) Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 280:22809-22818.
    • (2005) J Biol Chem , vol.280 , pp. 22809-22818
    • Gokhale, K.C.1    Newnam, G.P.2    Sherman, M.Y.3    Chernoff, Y.O.4
  • 26
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T, Wilkinson AJ (2001) AAA+ superfamily ATPases: Common structure-diverse function. Genes Cells 6:575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 27
    • 0037162510 scopus 로고    scopus 로고
    • Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
    • Jung G, Jones G, Masison DC (2002) Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci USA 99:9936-9941.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9936-9941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 28
    • 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
  • 29
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez Y, Lindquist SL (1990) HSP104 required for induced thermotolerance. Science 248:1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 30
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 33
    • 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
  • 34
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 35
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.