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Originally published as Genetics Published Articles Ahead of Print on November 4, 2005.
Genetics, Vol. 172, 827-835, February 2006, Copyright © 2006
doi:10.1534/genetics.105.048660
The Role of the N-Terminal Oligopeptide Repeats of the Yeast Sup35 Prion Protein in Propagation and Transmission of Prion Variants
Irina S. Shkundina*,
Vitaly V. Kushnirov*,
Mick F. Tuite
and
Michael D. Ter-Avanesyan*,1
* Institute of Experimental Cardiology, Cardiology Research Center, 121552 Moscow, Russia and Department of Biosciences, University of Kent, Canterbury CT2 7NJ, United Kingdom
1 Corresponding author: Institute of Experimental Cardiology, Cardiology Research Center, 3rd Cherepkovskaya str. 15A, 121552 Moscow, Russia.
E-mail: mdter{at}cardio.ru
The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein. Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves fragmentation of Sup35 polymers by the chaperone Hsp104. The nonsense suppressor [PSI+] phenotype can vary in efficiency probably due to different inheritable Sup35 polymer structures. Here we study the ability of Sup35 mutants with various deletions of the oligopeptide repeats to support [PSI+] propagation. We define the minimal region of the Sup35–PrD necessary to support [PSI+] as amino acids 1–64, which include the first two repeats, although a longer fragment, 1–83, is required to maintain weak [PSI+] variants. Replacement of wild-type Sup35 with deletion mutants decreases the strength of the [PSI+] phenotype. However, with one exception, reintroducing the wild-type Sup35 restores the original phenotype. Thus, the specific prion fold defining the [PSI+] variant can be preserved by the mutant Sup35 protein despite the change of phenotype. Coexpression of wild-type and mutant Sup35 containing three, two, one, or no oligopeptide repeats causes variant-specific [PSI+] elimination. These data suggest that [PSI+] variability is primarily defined by differential folding of the Sup35–PrD oligopeptide-repeat region.
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