Staniforth, G.L. and Tuite, M.F. (2012) Fungal Prions. In: Molecular Biology of Neurodegenerative Diseases. Progress in Molecular Biology and Translational Science, 107 . Elsevier, pp. 417-456. ISBN 978012385883-2.
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For both mammalian and fungal prion proteins, conformational templating drives the phenomenon of protein-only infectivity. The conformational conversion of a protein to its transmissible prion state is associated with changes to host cellular physiology. In mammals, this change is synonymous with disease, whereas in fungi no notable detrimental effect on the host is typically observed. Instead, fungal prions can serve as epigenetic regulators of inheritance in the form of partial loss-of-function phenotypes. In the presence of environmental challenges, the prion state [PRION+], with its resource for phenotypic plasticity, can be associated with a growth advantage. The growing number of yeast proteins that can switch to a heritable [PRION+] form represents diverse and metabolically penetrating cellular functions, suggesting that the [PRION+] state in yeast is a functional one, albeit rarely found in nature. In this chapter, we introduce the biochemical and genetic properties of fungal prions, many of which are shared by the mammalian prion protein PrP, and then outline the major contributions that studies on fungal prions have made to prion biology.
|Item Type:||Book section|
|Uncontrolled keywords:||Prion; Yeast; Saccharomyces cerevisiae; Molecular chaperone; [PSI+] prion; [URE3] prion; [PIN+] prion|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||24 Apr 2012 10:34|
|Last Modified:||24 Apr 2012 11:08|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/29322 (The current URI for this page, for reference purposes)|
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