The relationship of prions and translation

Wiley Interdiscip Rev RNA. 2010 Jul-Aug;1(1):81-9. doi: 10.1002/wrna.8.

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.

Keywords: Sup35; amyloid; chaperones; mRNA turnover; parallel in-register; prion; translation termination.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Animals
  • Humans
  • Mammals / genetics
  • Mammals / metabolism
  • Models, Biological
  • Peptide Termination Factors / genetics
  • Peptide Termination Factors / metabolism
  • Peptide Termination Factors / physiology
  • Prions / genetics
  • Prions / metabolism
  • Prions / physiology*
  • Protein Biosynthesis / genetics*
  • Regulatory Sequences, Ribonucleic Acid / genetics
  • Regulatory Sequences, Ribonucleic Acid / physiology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology

Substances

  • Peptide Termination Factors
  • Prions
  • Regulatory Sequences, Ribonucleic Acid
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins