Yeast prions

Lansbury PT Jr. Yeast prions inheritance by seeded protein polymerization Curr Biol 1997 7 R617-R619. 

Fig. 4. New structural models for amyloid and prion filaments with the parallel and in-register arrangement of //-strands in the //-sheets. //-Strands are denoted by arrows. The filaments are formed by hydrogen-bonded stacks of repetitive units. Axial projections of single repetitive units corresponding to each model are shown on the top. Lateral views of the overall structures are on the bottom. (A) The core of a //-helical model of the //-amyloid protofilament (Petkova et al., 2002). Two such protofilaments coil around one another to form a //-amyloid fibril. (B) The core of a //-helical model of the HET-s prion fibril (Ritter et al., 2005). The repetitive unit consists of two //-helical coils. (C) The core of a superpleated //-structura l model suggested for yeast prion Ure2p protofilaments and other amyloids (Kajava et al., 2004).

Chan,J. C., Oyler, N. A., Yau, W. M., and Tycko, R. (2005). Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44, 10669-10680. 

Kishimoto, A., Hasegawa, K., Suzuki, H., Taguchi, H., Namba, K., and Yoshida, M. (2004). Beta-helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem. Biophys. Res. Commun. 315, 739-745. 

We now summarize current experimentally derived constraints that models of yeast prion filaments must satisfy in addition to the basic requirement of cross-/) structure and then go on in Section VI to discuss their implications for several models that have been proposed. 

A third yeast prion, PIN, is similar in some respects, but its non-prion domain—in this case, the N-terminal part of the molecule—has no established cellular function. The protein Rnqlp is a gain-of-function prion whose activity is expressed via its ability to induce [PS/]. [PIN] forms much more readily than the other two prions, and [PIN] cells induce [PSI] under... 

Bai, M., Zhou, J. M., and Perrett, S. (2004). The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J. Biol. Chem. 279, 50025-50030. 

Bousset, L., Belrhali, H., Melki, R., and Morera, S. (2001b). Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40, 13564-13573. 

Bousset, L., Thomson, N. H., Radford, S. E., and Melki, R. (2002). The yeast prion Ure2p retains its native a-helical conformation upon assembly into protein fibrils in vitro. EMBOJ. 21, 2903-2911. 

DePace, A. H., and Weissman, J. S. (2002). Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat. Struct. Biol. 9, 389-396. 

Diaz-Avalos, R., King, C. Y., Wall,J., Simon, M., and Caspar, D. L. (2005). Strain-specific morphologies of yeast prion amyloid fibrils. Proc. Natl. Acad. Sci. USA 102, 10165-10170. 

Fay, N., Inoue, Y., Bousset, L., Taguchi, H., and Melki, R. (2003). Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization. /. Biol. Chem. 278, 30199-30205. 

Inoue, Y., Kishimoto, A., Hirao, J., Yoshida, M., and Taguchi, H. (2001). Strong growth polarity of yeast prion fiber revealed by single fiber imaging. /. Biol. Chem. 276, 35227-35230. 

Krishnan, R., and Lindquist, S. L. (2005). Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772. 

Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N., and Ter-Avanesyan, M. D. (1996). Propagation of the yeast prion-like psi] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134. 

Schlumpberger, M., Prusiner, S. B., and Herskowitz, I. (2001). Induction of distinct [URE3] yeast prion strains. Mol. Cell. Biol. 21, 7035-7046. 

Stability, folding, dimerization, and assembly properties of the yeast prion... 

Tuite, M. F. (2000). Yeast prions and their prion-forming domain. Cell 100, 289-292. Tycko, R. (2000). Solid-state NMR as a probe of amyloid fibril structure. Curr. Opin. Chem. Biol. 4, 500-506. 

Umland, T. C., Taylor, K. L., Rhee, S., Wickner, R. B., and Davies, D. R. (2001). The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA 98, 1459-1464. 

GNNQQNY Yeast prion Sup35 /1-Sheet Balbirnie et al. (2001) ... 

Balbirnie, M., Grothe, R., and Eisenberg, D. S. (2001). An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. 

Diaz-Avalos, R., King, C. Y., Wall,J., Simon, M., and Caspar, D. L. (2005). Strain-specific morphologies of yeast prion amyloid fibrils. Proc. Natl. Acad. Sci. USA 102,10165-10170. Donne, D. G., Viles, J. H., Groth, D., Mehlhom, I., James, T. L., Cohen, F. E., Prusiner, S. B., Wright, P. E., and Dyson, H.J. (1997). Structure of the recombinant full-length hamster prion protein PrP(29-231) The N terminus is highly flexible. Proc. Natl. Acad. Sci. USA 94, 13452-13457. 

In a later publication, Kishimoto et al. (2004) proposed the water-filled nanotube as a model for the fibrillar N-terminal domain of the yeast prion Sup35p. The authors find that hydrated Sup35p fibrils show no 10-A equatorial reflection in the fiber diffraction pattern, but that dried fibrils... 

Komar, A. A., Melki, R., and Cullin, C. (1999). The [URE3] yeast prion From genetics to biochemistry. Biochemistry (Mosc.) 64, 1401-1407. 

K. D. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool, J Biol Chem, 2003, 278, 52102-15. 

DePace AH, Santoso A, Hillner P, Weissman JS (1998) A critical role for amino-terminal glu-tamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93 1241-1252 Didichenko SA, Ter-Avanesyan MD, Smirnov VN (1991) Ribosome-bound EF-1 alpha-like protein of yeast Saccharomyces cerevisiae. Eur J Biochem 198 705-711 Dong H, Kurland CG (1995) Ribosome mutants with altered accuracy translate with reduced processivity. J Mol Biol 248 551-561... 

True HE, Lindquist SL (2000) A yeast prion provides a mechanism for genetic variation and phenotypic... 

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