Prion propagation and inositol polyphosphates

Curr Genet. 2018 Jun;64(3):571-574. doi: 10.1007/s00294-017-0788-2. Epub 2017 Dec 14.

Abstract

The [PSI+] prion is a folded in-register parallel β-sheet amyloid (filamentous polymer) of Sup35p, a subunit of the translation termination factor. Our searches for anti-prion systems led to our finding that certain soluble inositol polyphosphates (IPs) are important for the propagation of the [PSI+] prion. The IPs affect a wide range of processes, including mRNA export, telomere length, phosphate and polyphosphate metabolism, energy regulation, transcription and translation. We found that 5-diphosphoinositol tetra(or penta)kisphosphate or inositol hexakisphosphate could support [PSI+] prion propagation, and 1-diphosphoinositol pentakisphosphate appears to inhibit the process.

Keywords: Inositol polyphosphate; Prion; Siw14; Sup35; [PSI+].

Publication types

  • Review

MeSH terms

  • Energy Metabolism
  • Inositol / chemistry*
  • Polyphosphates / chemistry
  • Polyphosphates / metabolism*
  • Prions / genetics*
  • Protein Biosynthesis
  • RNA, Fungal / genetics
  • RNA, Messenger / genetics
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Telomere
  • Transcription, Genetic

Substances

  • Polyphosphates
  • Prions
  • RNA, Fungal
  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins
  • Inositol