Prion proteins are found in mammals and @entity375 , and can transmit diseases and encode heritable phenotypic traits. In @entity375 , eRF3, @entity43855 , @entity23264 and Swil are functional proteins with a soluble conformation that can switch to a non-functional, amyloid conformation denoted as [PSI+], [PIN+], [URE3] and [SWI+], respectively. The prion [PSI+] corresponds to an aggregated conformation of the translational release factor eRF3, which suppresses nonsense codons. [PSI+] modifies cellular fitness and induces several phenotypes according to the genetic background. An elegant series of studies has demonstrated that several [PSI+]-induced phenotypes occur as a consequence of decreased translational termination efficiency. However, the genes whose expression levels are controlled by [PSI+] remain largely unknown. Here, we show that [PSI+] enhances expression of antizyme, a negative regulator of cellular @entity4663 , by modulating the +1 frameshifting required for its expression. Our study also demonstrates that [PSI+] greatly affects cellular @entity4663 in @entity375 . We show that modification of the cellular content of @entity4663 by the prion accounts for half of the [PSI+]-induced phenotypes. Antizyme is the first protein to be described for which expression of its functional form is stimulated by [PSI+].

Epigenetic control of XXXX by the prion [PSI+].

@entity23264 :: ('855492(Tax:4932)', 'Gene') :: ['Ure2'] @entity375 :: ('4932', 'Species') :: ['yeast', 'Saccharomyces cerevisiae'] @entity43855 :: ('850329(Tax:4932)', 'Gene') :: ['Rnq1'] @entity4663 :: ('MESH:D011073', 'Chemical') :: ['polyamines']
@entity4663 :: (MESH:D011073,Chemical) :: ['polyamines']
