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Yeast prions: Paramutation at the protein level?

Tuite, Mick F. (2015) Yeast prions: Paramutation at the protein level? Seminars in Cell & Developmental Biology, 44 . pp. 51-61. ISSN 1084-9521. (doi:10.1016/j.semcdb.2015.08.016) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:52262)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://doi.org/10.1016/j.semcdb.2015.08.016

Abstract

Prions are proteins that have the potential to refold into a novel conformation that templates the conversion of like molecules to the altered infectious form. In the yeast Saccharomyces cerevisiae, trans-generational epigenetic inheritance can be mediated by a number of structurally and functionally diverse prions. Prionogenesis can confer both loss-of-function and gain-of-function properties to the prion protein and this in turn can have a major impact on host phenotype, short-term adaptation and evolution of new traits. Prionogenesis shares a number of properties in common with paramutation and can be considered as a mitotically and meiotically heritable change in protein conformation induced by trans-interactions between homologous proteins.

Item Type: Article
DOI/Identification number: 10.1016/j.semcdb.2015.08.016
Uncontrolled keywords: Prions; Epigenetic inheritance; Amyloid; Yeast; Saccharomyces cerevisiae; Propagons; Prion variants; Transcription factors; Protein conformation; Conformational conversion
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Susan Davies
Date Deposited: 23 Nov 2015 15:10 UTC
Last Modified: 06 May 2020 03:13 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/52262 (The current URI for this page, for reference purposes)
Tuite, Mick F.: https://orcid.org/0000-0002-5214-540X
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