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The relationship of prions and translation

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Abstract Prions are infectious proteins, without the need for an accompanying nucleic acid. Nonetheless, there are connections of prions with translation and RNA, which we explore here. Most prions are based on self‐propagating amyloids. The yeast [PSI+] prion is an amyloid of Sup35p, a subunit of the translation termination factor. The normal function of the Sup35p prion domain is in shortening the 3′ polyA of mRNAs and thus in mRNA turnover. The [ISP+] prion is so named because it produces antisuppression, the opposite of the effect of [PSI+]. Another connection of prions with translation is the influence on prion propagation and generation of ribosome‐associated chaperones, the Ssbs, and a chaperone activity intrinsic to the 60S ribosomal subunits. Copyright © 2010 John Wiley & Sons, Ltd. This article is categorized under: Translation > Translation Mechanisms Translation > Translation Regulation

In‐register parallel β‐sheet structure explains how prions transmit their conformation to the normal form of the protein. The unstructured prion domain of monomers is forced to assume the conformation of the protein in the amyloid filaments by interactions with the main chain and side chain parts of the identical residues of the protein, shown by the red dots.

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Prions and translation. The Sup35 prion protein is a component of the translation termination factor, and is necessary for the shortening of the 3′ polyA of mRNAs that is a stage in mRNA degradation. The ribosome‐associated Ssb1 chaperone protein and the chaperone activity of the 60S ribosome subunits also affect prion generation and propagation. The [ISP+] prion also affects translation by an as yet unknown mechanism.

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