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. | |
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 |
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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 > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 23 Nov 2015 15:10 UTC |
Last Modified: | 05 Nov 2024 10:38 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/52262 (The current URI for this page, for reference purposes) |
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