Prion-forming domains

Nazabal, A., Maddelein, M. L., Bonneu, M., Saupe, S. J., and Schmitter, J. M. (2005). Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry./ Biol. Chem. 280, 13220-13228. 

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. 

Bailleul PA, Newnam GP, Steenbergen JN, Chernoff YO (1999) Genetic study of interactions between the cytoskeletal assembly protein slal and prion-forming domain of the release factor Sup35 (eRF3) in Sac-charomyces cerevisiae. Genetics 153 81-94... 

True HE, Berlin 1, Lindquist SL (2004) Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431 184—187 Tuite ME (2000) Yeast prions and their prion-forming domain. Cell 100 289—292... 

Tuite MF (2000) Yeast prions and their prion-forming domain. Cell 100 289-292... 

As for HET-s, the structure of its N-terminal domain has yet to be determined however, NMR data suggest that residues 1-227 form a well-folded domain (Balguerie et al, 2003). HET-s is a special case because the prion form is the active form, so that the prion domain (residues 218-289) is needed for function. Although the prion domain alone is sufficient for prion maintenance, it is not competent in heterokaryon incompatibility. For this activity, at least HET-s157-289 must be expressed (Balguerie et al., 2004). 

A cross-// spine structure consists of two or more flat or twisted //-sheets, composed of parallel (Nelson et al., 2005) or antiparallel (Makin et al., 2005) //-strands, in a cross-/ arrangement. The cross-/ spine model of fibril formation proposes that a short segment of the native protein changes conformation to form one or more //-strands of a cross-/ spine. The seven-residue peptide GNNQQNY, derived from the prion-determining domain... 

D. Prion Domains Form the Filament Backbone Other Domains Are... 

All fungal prion proteins have a so-called prion domain and a functional domain. The prion domain is a region of the polypeptide chain that is necessary and sufficient for prion formation and maintenance (Fig. 1 Wickner et al., 2002). For Ure2p and Sup35p, the functional domain is responsible for the cellular activity of the normal form of the protein. 

Chimeras in which the prion domains of Ure2p and Sup35p are fused with other unrelated proteins also form filaments (Baxa et al., 2002 Diaz-Avalos et al., 2005 King and Diaz-Avalos, 2004 Schlumpberger et al, 2000)... 

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... 

Baxa, U., Taylor, K. L., Wall, J. S., Simon, M. N., Cheng, N., Wickner, R. B., and Steven, A. C. (2003). Architecture of Ure2p prion filaments The N-terminal domains form a central core fiber./. Biol. Chem. 278, 43717-43727. 

Ross, E. D., Baxa, U., and Wickner, R. B. (2004). Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 24, 7206-7213. 

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