메뉴 건너뛰기




Volumn 12, Issue 4, 2013, Pages 551-558

The [URE3] prion in Candida

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; GLUTATHIONE PEROXIDASE;

EID: 84874620417     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00015-13     Document Type: Article
Times cited : (17)

References (56)
  • 1
    • 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
  • 2
    • 0036024577 scopus 로고    scopus 로고
    • Transmitting the signal of excess nitrogen in Saccharo-myces cerevisiae from the Tor proteinstothe GATA factors: Connecting the dots
    • Cooper TG. 2002. Transmitting the signal of excess nitrogen in Saccharo-myces cerevisiae from the Tor proteinstothe GATA factors: connecting the dots. FEMS Microbiol. Rev. 26:223-238.
    • (2002) FEMS Microbiol. Rev , vol.26 , pp. 223-238
    • Cooper, T.G.1
  • 3
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in S. cerevisiae
    • Wickner RB. 1994. [URE3] as an altered URE2 protein: evidence for a prion analog in S. cerevisiae. Science 264:566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 4
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison DC, Wickner RB. 1995. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270: 93-95.
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 5
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor KL, Cheng N, Williams RW, Steven AC, Wickner RB. 1999. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283:1339-1343.
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 6
    • 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
  • 7
    • 34547136725 scopus 로고    scopus 로고
    • Ure2p function is enhanced by its prion domain in Saccharomyces cerevi-siae
    • Shewmaker F, Mull L, Nakayashiki T, Masison DC, Wickner RB. 2007. Ure2p function is enhanced by its prion domain in Saccharomyces cerevi-siae. Genetics 176:1557-1565.
    • (2007) Genetics , pp. 1557-1565
    • Shewmaker, F.1    Mull, L.2    Nakayashiki, T.3    Masison, D.C.4    Wickner, R.B.5
  • 9
    • 0030780097 scopus 로고    scopus 로고
    • The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
    • Masison DC, Maddelein Wickner M-LRB. 1997. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc. Natl. Acad. Sci. U. S. A. 94:12503-12508.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 12503-12508
    • Masison, D.C.1    Maddelein Wickner, M.-L.R.B.2
  • 11
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson D, Marekov L, Yau Tycko W-MR. 2007. Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance. Biochemistry 46: 13149-13162.
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.4    Marekov, L.5    Yau Tycko, W.-M.R.6
  • 12
    • 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
  • 15
    • 79960007397 scopus 로고    scopus 로고
    • Amyloid of the Candida albicans Ure2p prion domain is infectious and has a parallel in-register β-sheet structure
    • Engel A, Shewmaker F, Edskes HK, Dyda F, Wickner RB. 2011. Amyloid of the Candida albicans Ure2p prion domain is infectious and has a parallel in-register β-sheet structure. Biochemistry 50:5971-5978.
    • (2011) Biochemistry , vol.50 , pp. 5971-5978
    • Engel, A.1    Shewmaker, F.2    Edskes, H.K.3    Dyda, F.4    Wickner, R.B.5
  • 18
  • 19
    • 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. 2001. Yeast [PSI+] "prions" that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol. Cell 7:1121-1130.
    • (2001) Mol. Cell , vol.7 , pp. 1121-1130
    • Nakayashiki, T.1    Ebihara, K.2    Bannai, H.3    Nakamura, Y.4
  • 20
    • 78651492351 scopus 로고    scopus 로고
    • Yeast prions: Could they be exaptations? The URE2/[URE3] system in Kluyveromyces lactis
    • Safadi RA, Talarek N, Jacques N, Aigle M. 2011. Yeast prions: could they be exaptations? The URE2/[URE3] system in Kluyveromyces lactis. FEMS Yeast Res. 11:151-153.
    • (2011) FEMS Yeast Res , vol.11 , pp. 151-153
    • Safadi, R.A.1    Talarek, N.2    Jacques, N.3    Aigle, M.4
  • 21
    • 26444520003 scopus 로고    scopus 로고
    • The [URE3] prion is not conserved among Saccharomyces species
    • Talarek N, Maillet L, Cullin C, Aigle M. 2005. The [URE3] prion is not conserved among Saccharomyces species. Genetics 171:23-54.
    • (2005) Genetics , vol.171 , pp. 23-54
    • Talarek, N.1    Maillet, L.2    Cullin, C.3    Aigle, M.4
  • 24
    • 0142216842 scopus 로고    scopus 로고
    • Transformation of yeast by the Liac/SS carrier DNA/PEG method
    • Geitz RD, Woods RA. 2002. Transformation of yeast by the Liac/SS carrier DNA/PEG method. Methods Enzymol. 350:87-96.
    • (2002) Methods Enzymol , vol.350 , pp. 87-96
    • Geitz, R.D.1    Woods, R.A.2
  • 25
    • 0032981335 scopus 로고    scopus 로고
    • Efficient homologous and illegitimate recombination in the opportunistic yeast pathogen Candida glabrata
    • Cormack BP, Falkow S. 1999. Efficient homologous and illegitimate recombination in the opportunistic yeast pathogen Candida glabrata. Genetics 151:979-987.
    • (1999) Genetics , vol.151 , pp. 979-987
    • Cormack, B.P.1    Falkow, S.2
  • 27
    • 34250617570 scopus 로고    scopus 로고
    • A family of glycosylphosphatidyl-inositol-linked aspartyl proteases is required for virulence of Candida glabrata
    • Kaur R, Ma B, Cormack BP. 2007. A family of glycosylphosphatidyl-inositol-linked aspartyl proteases is required for virulence of Candida glabrata. Proc. Natl. Acad. Sci. U. S. A. 104:7628-7633.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 7628-7633
    • Kaur, R.1    Ma, B.2    Cormack, B.P.3
  • 29
    • 34147156603 scopus 로고    scopus 로고
    • Polyamine uptake by DUR3 and SAM3 in Saccharomyces cerevisiae
    • Uemura T, Kashiwagi K, Igarashi K. 2007. Polyamine uptake by DUR3 and SAM3 in Saccharomyces cerevisiae. J. Biol. Chem. 282:7733-7741.
    • (2007) J. Biol. Chem , vol.282 , pp. 7733-7741
    • Uemura, T.1    Kashiwagi, K.2    Igarashi, K.3
  • 30
  • 31
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 32
    • 0028266417 scopus 로고
    • A system for gene cloning and manipulation in the yeast Candida glabrata
    • Zhou P, Szczypka MS, Young R, Thiele DJ. 1994. A system for gene cloning and manipulation in the yeast Candida glabrata. Gene 142:135-140.
    • (1994) Gene , vol.142 , pp. 135-140
    • Zhou, P.1    Szczypka, M.S.2    Young, R.3    Thiele, D.J.4
  • 33
    • 0032510821 scopus 로고    scopus 로고
    • A high-copy-number ADE2-bearing plasmid for transformation of Candida glabrata
    • Hanic-Joyce PJ, Joyce PB. 1998. A high-copy-number ADE2-bearing plasmid for transformation of Candida glabrata. Gene 211:395-400.
    • (1998) Gene , vol.211 , pp. 395-400
    • Hanic-Joyce, P.J.1    Joyce, P.B.2
  • 34
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet T, Dignard D, Thomas DY. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 35
    • 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
  • 38
    • 0021706678 scopus 로고
    • Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae
    • Mitchell AP, Magasanik B. 1984. Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae. Mol. Cell. Biol. 4:2758-2766.
    • (1984) Mol. Cell. Biol , vol.4 , pp. 2758-2766
    • Mitchell, A.P.1    Magasanik, B.2
  • 39
    • 47049120414 scopus 로고    scopus 로고
    • The asexual yeast Candida glabrata maintains distinct a and a haploid mating types
    • Muller H, Hennequin C, Gallaud J, Dujon B, Fairhead C. 2008. The asexual yeast Candida glabrata maintains distinct a and a haploid mating types. Eukaryot. Cell 7:848-858.
    • (2008) Eukaryot. Cell , vol.7 , pp. 848-858
    • Muller, H.1    Hennequin, C.2    Gallaud, J.3    Dujon, B.4    Fairhead, C.5
  • 41
    • 0345283057 scopus 로고    scopus 로고
    • Phenotypic switching and mating type switching of Candida glabrata at sites of colonization
    • Brockert PJ, Lachke SA, Srikantha T, Pujol C, Galask R, Soll DR. 2003. Phenotypic switching and mating type switching of Candida glabrata at sites of colonization. Infect. Immun. 71:7109-7118.
    • (2003) Infect. Immun , vol.71 , pp. 7109-7118
    • Brockert, P.J.1    Lachke, S.A.2    Srikantha, T.3    Pujol, C.4    Galask, R.5    Soll, D.R.6
  • 43
    • 32944457631 scopus 로고    scopus 로고
    • The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans
    • Zenthon JF, Ness F, Cox B, Tuite MF. 2006. The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans. Eukaryot. Cell 5:217-225.
    • (2006) Eukaryot. Cell , vol.5 , pp. 217-225
    • Zenthon, J.F.1    Ness, F.2    Cox, B.3    Tuite, M.F.4
  • 44
    • 33745585095 scopus 로고    scopus 로고
    • Reporter assay systems for [URE3] detection and analysis
    • Brachmann A, Toombs JA, Ross ED. 2006. Reporter assay systems for [URE3] detection and analysis. Methods 39:35-42.
    • (2006) Methods , vol.39 , pp. 35-42
    • Brachmann, A.1    Toombs, J.A.2    Ross, E.D.3
  • 45
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S. 2005. Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6:435-450.
    • (2005) Nat. Rev. Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 46
  • 47
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • Ross ED, Baxa U, Wickner RB. 2004. Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 24:7206-7213.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 49
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs JA, McCarty BR, Ross ED. 2010. Compositional determinants of prion formation in yeast. Mol. Cell. Biol. 30:319-332.
    • (2010) Mol. Cell. Biol , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 50
    • 0037301367 scopus 로고    scopus 로고
    • Multiple amino acid residues within the rabbit PrP protein inhibit formation of its abnormal isoform
    • Vorberg I, Groschup MH, Pfaff E, Priola SA. 2003. Multiple amino acid residues within the rabbit PrP protein inhibit formation of its abnormal isoform. J. Virol. 77:2003-2009.
    • (2003) J. Virol , vol.77 , pp. 2003-2009
    • Vorberg, I.1    Groschup, M.H.2    Pfaff, E.3    Priola, S.A.4
  • 51
    • 0033955802 scopus 로고    scopus 로고
    • The role of ammonia metabolism in nitrogen catabolite repression in Saccharomyces cerevisiae
    • ter Schure EG, van Riel NA, Verrips CT. 2000. The role of ammonia metabolism in nitrogen catabolite repression in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 24:67-83.
    • (2000) FEMS Microbiol. Rev , vol.24 , pp. 67-83
    • ter Schure, E.G.1    van Riel, N.A.2    Verrips, C.T.3
  • 52
    • 0032750741 scopus 로고    scopus 로고
    • Nitrogen catabolite repression in Saccharomyces cerevisiae
    • Hofman-Bang J. 1999. Nitrogen catabolite repression in Saccharomyces cerevisiae. Mol. Biotech. 12:35-71.
    • (1999) Mol. Biotech , vol.12 , pp. 35-71
    • Hofman-Bang, J.1
  • 53
    • 4644362697 scopus 로고    scopus 로고
    • Synergistic operation of four cis-acting elements mediate high level DAL5 transcription in Saccharomyces cerevisiae
    • Rai R, Daugherty JR, Tate JJ, Buford TD, Cooper TG. 2004. Synergistic operation of four cis-acting elements mediate high level DAL5 transcription in Saccharomyces cerevisiae. FEMS Yeast Res. 5:29-41.
    • (2004) FEMS Yeast Res , vol.5 , pp. 29-41
    • Rai, R.1    Daugherty, J.R.2    Tate, J.J.3    Buford, T.D.4    Cooper, T.G.5
  • 54
    • 0028876606 scopus 로고
    • Transcriptional and posttranscrip-tional regulation of the general amino acid permease of Saccharomyces cerevisiae
    • Stanbrough M, Magasanik B. 1995. Transcriptional and posttranscrip-tional regulation of the general amino acid permease of Saccharomyces cerevisiae. J. Bacteriol. 177:94-102.
    • (1995) J. Bacteriol , vol.177 , pp. 94-102
    • Stanbrough, M.1    Magasanik, B.2
  • 55
    • 33745615846 scopus 로고    scopus 로고
    • Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway
    • Rubio-Texeira M, Kaiser CA. 2006. Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway. Mol. Biol. Cell 17:3031-3050.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3031-3050
    • Rubio-Texeira, M.1    Kaiser, C.A.2
  • 56
    • 0015056102 scopus 로고
    • Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast
    • Lacroute F. 1971. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106:519-522.
    • (1971) J. Bacteriol , vol.106 , pp. 519-522
    • Lacroute, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.