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The relationship of prions and translation

Authors :
Wickner, Reed B.
Edskes, Herman K.
Shewmaker, Frank P.
Kryndushkin, Dmitry
Nemecek, Julie
McGlinchey, Ryan
Bateman, David
Source :
Wiley Interdisciplinary Reviews: RNA; July 2010, Vol. 1 Issue: 1 p81-89, 9p
Publication Year :
2010

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.

Details

Language :
English
ISSN :
17577004 and 17577012
Volume :
1
Issue :
1
Database :
Supplemental Index
Journal :
Wiley Interdisciplinary Reviews: RNA
Publication Type :
Periodical
Accession number :
ejs21703297
Full Text :
https://doi.org/10.1002/wrna.8