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Podospora anserina

Balguerie, A., Dos Reis, S., Ritter, C., Chaignepain, S., Coulary-Salin, B., Forge, V., Bathany, K., Lascu, I., Schmitter, J. M., Riek, R., and Saupe, S. J. (2003). Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J. 22, 2071-2081. [Pg.172]

Coustou, V., Deleu, C., Saupe, S., and Begueret, J. (1997). The protein product of the Ziet-sheterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. USA 94, 9773-9778. [Pg.174]

Fig. 4. Comparison of Mad and Mad orthologues from Podospora anserina (Grisea) and Schizosaccharomyces pom.be (Cufl). All contain a conserved N-terminal 40-residue Zn(II) module that constitutes part of the DNA-hinding interface. Two Cys-rich motifs in the C-terminal segment of Mad, designated Cl and C2, are conserved in Grisea and Cufl. The Cl and C2 motifs are part of transactivation domains. The Cl motif is a functional Cu-regulatory domain in Mad. The sequence of the Cl motif is shown at the top. The dark ovals represent the positions of cysteinyl residues in each molecule. Each Cys-rich motif in Mad hinds four Cu(l) ions. Fig. 4. Comparison of Mad and Mad orthologues from Podospora anserina (Grisea) and Schizosaccharomyces pom.be (Cufl). All contain a conserved N-terminal 40-residue Zn(II) module that constitutes part of the DNA-hinding interface. Two Cys-rich motifs in the C-terminal segment of Mad, designated Cl and C2, are conserved in Grisea and Cufl. The Cl and C2 motifs are part of transactivation domains. The Cl motif is a functional Cu-regulatory domain in Mad. The sequence of the Cl motif is shown at the top. The dark ovals represent the positions of cysteinyl residues in each molecule. Each Cys-rich motif in Mad hinds four Cu(l) ions.
Fig. 6. Occurrence of the CXCX(4 5) CXC consensus motif. CopY, cop operon repressor protein from Enterococcus hirae Mad, transcription factor for the Ctrl copper transporter of Saccharomyces cerevisiae AMTl, transcription factor for metal-lothionein from Candida albicans ACEl, transcription factor for metallothionein from Sa. cerevisiae Grisea, MACl orthologue of Podospora anserina MT-2 p-domain, N-terminal domain of human metallothionein-2. Fig. 6. Occurrence of the CXCX(4 5) CXC consensus motif. CopY, cop operon repressor protein from Enterococcus hirae Mad, transcription factor for the Ctrl copper transporter of Saccharomyces cerevisiae AMTl, transcription factor for metal-lothionein from Candida albicans ACEl, transcription factor for metallothionein from Sa. cerevisiae Grisea, MACl orthologue of Podospora anserina MT-2 p-domain, N-terminal domain of human metallothionein-2.
Saupe SJ, Descamps C, Turcq B, Begueret J Inactivation of the Podospora anserina vegetative incompatibility locus het-c, whose product resembles a glycolipid transfer protein, drastically impairs ascospore production. Proc Natl Acad Sci USA 1994 91 5927-5931. [Pg.280]

Keywords Molecular chaperone Podospora anserina Prion Prion propagation Propagons Yeast Saccharomyces cerevisiae)... [Pg.257]

Coustou-Linares V, Maddelein ML, Begueret J, Saupe SJ (2001) In vivo aggregation of the HET-s prion protein of the fungus Podospora anserina. Mol Microbiol 42 1325-1335... [Pg.290]

Saupe SJ (2007) A short history of small s a prion of the fungus Podospora anserina. Prion 1 110-115... [Pg.291]

X. [Het-s], A Prion of the Fungus Podospora anserina. Is Necessary FOR A Normal Function... [Pg.325]

Fig. 8. The [Het-s] prion of Podospora anserina is necessary for heterokaryon incompatibility, a normal cellular function (Coustou et al., 1997). Fig. 8. The [Het-s] prion of Podospora anserina is necessary for heterokaryon incompatibility, a normal cellular function (Coustou et al., 1997).
BeissonlSchecroun, J. (1962). Incompatibilte cellulaire et interactions nucleo-cytoplas-miques dans les phenomenes de barrage chez Podospora anserina. Ann. Genet. 4, 3-50. [Pg.330]

Rizet, G. (1952). Les phenomenes de barrage chez Podospora anserina analyse genetique des barrages entre les souches s et S. Rev. Cytol Biol Veg. 13, 51-92. [Pg.333]

Eric Dufour, Joceline Boulay, Vincent Rincheval, Annie Sainsard-Chanet, A causal link between resphation and senescence in Podospora anserina. Proceedings of the National Academy of Sciences USA, 97 (2000), 4138 143. [Pg.290]

R469 S. J. Saupe, The [Het-s] Prion of Podospora Anserina and Its Role in Heterokaryon Incompatibility , Semin. Cell Dev. Biol., 2011, 22, 460. [Pg.53]


See other pages where Podospora anserina is mentioned: [Pg.36]    [Pg.126]    [Pg.128]    [Pg.174]    [Pg.259]    [Pg.105]    [Pg.280]    [Pg.257]    [Pg.259]    [Pg.259]    [Pg.266]    [Pg.290]    [Pg.294]    [Pg.313]    [Pg.329]    [Pg.331]    [Pg.331]    [Pg.105]    [Pg.105]    [Pg.18]    [Pg.62]    [Pg.254]    [Pg.94]    [Pg.137]   
See also in sourсe #XX -- [ Pg.259 ]

See also in sourсe #XX -- [ Pg.257 , Pg.259 ]

See also in sourсe #XX -- [ Pg.105 ]

See also in sourсe #XX -- [ Pg.105 ]




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Podospora anserina prions

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Prion of the Fungus Podospora anserina, Is Necessary for a Normal Function

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