Prions cause infectious neurodegenerative diseases in mammals and control heritable traits in yeast . Most prions identified so far are self-polymerized amyloids that form highly ordered cross-β fibrous aggregates. The yeast prion [ PSI + ] is a self-perpetuating amyloid of Sup35 (also called eRF3), an evolutionarily conserved eukaryotic release factor that is required for the termination of translation . In its amyloid form, Sup35 function is impaired, resulting in the read-through of termination codons, and in some cases in a change in the reading frame , thereby allowing the bypassing of a stop codon, a process called translational frameshifting. Although this effect is deleterious under normal conditions, it has been proposed to have an adaptive role by generating extended proteins that may increase the evolutionary plasticity of the population . Indeed, the presence of [ PSI + ] was shown to generate phenotypic characteristics that increase the survival of some laboratory strains under certain conditions . However, it remained unknown which specific proteins contribute to these phenotypes. On page 1069 of this issue, Namy et al . provide an example of a programmed frameshifting that is modulated by [ PSI + ]. Programmed frameshifting occurs at specific
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Prion: disease or relief?
Chernoff, Yury O.
Follow Nature Cell Biology
, Volume 10 (9)
Nature Publishing Group (NPG) – Sep 1, 2008
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