| Literature DB >> 29243174 |
Reed B Wickner1, Herman K Edskes2, Evgeny E Bezsonov2, Moonil Son2, Mathieu Ducatez2.
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.Entities:
Keywords: Inositol polyphosphate; Prion; Siw14; Sup35; [PSI+]
Mesh:
Substances:
Year: 2017 PMID: 29243174 PMCID: PMC5949079 DOI: 10.1007/s00294-017-0788-2
Source DB: PubMed Journal: Curr Genet ISSN: 0172-8083 Impact factor: 3.886