Yeast Prions: Structure, Biology, and Prion-Handling Systems
Reed B. Wickner,Frank Shewmaker,David A. Bateman,Herman K. Edskes,Anton Gorkovskiy,Yaron Dayani,Evgeny E. Bezsonov +6 more
TLDR
The mechanism of faithful templating of protein conformation, the biological roles of these prions, and their interactions with cellular chaperones, the Btn2 and Cur1 aggregate-handling systems, and other cellular factors governing prion generation and propagation are reviewed.Abstract:
A prion is an infectious protein horizontally transmitting a disease or trait without a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of protein, generally an altered form of a protein that catalyzes the same alteration of the protein. Yeast prions are thus transmitted both vertically (as genes composed of protein) and horizontally (as infectious proteins, or prions). Formation of amyloids (linear ordered β-sheet-rich protein aggregates with β-strands perpendicular to the long axis of the filament) underlies most yeast and fungal prions, and a single prion protein can have any of several distinct self-propagating amyloid forms with different biological properties (prion variants). Here we review the mechanism of faithful templating of protein conformation, the biological roles of these prions, and their interactions with cellular chaperones, the Btn2 and Cur1 aggregate-handling systems, and other cellular factors governing prion generation and propagation. Human amyloidoses include the PrP-based prion conditions and many other, more common amyloid-based diseases, several of which show prion-like features. Yeast prions increasingly are serving as models for the understanding and treatment of many mammalian amyloidoses. Patients with different clinical pictures of the same amyloidosis may be the equivalent of yeasts with different prion variants.read more
Citations
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Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease.
TL;DR: This review highlights recent advances in understanding of the role of prions in enabling rapid adaptation to environmental stress in yeast and discusses the prevalence of the PrLD in nucleic-acid binding proteins that are often connected to neurodegenerative disease.
Journal ArticleDOI
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann,Simon Alberti +1 more
TL;DR: It is argued that prion-like low-complexity regions (LCRs) are key regulators of protein solubility and folding and that prions have evolved to regulate protein phase behavior and to protect proteins against proteotoxic damage.
Journal ArticleDOI
Protein aggregation as a mechanism of adaptive cellular responses
Juha Saarikangas,Yves Barral +1 more
TL;DR: Several protein bodies that differ in composition, packing, dynamics, size, and localization were originally discovered in budding yeast and are provided with a concise and comparative review of their nature and nomenclature.
Journal ArticleDOI
Yeast and Fungal Prions.
TL;DR: Yeast and fungal prions are infectious proteins, most being self-propagating amyloids of normally soluble proteins, an architecture that naturally suggests a mechanism by which a protein can template its conformation, just as DNA or RNA templates its sequence.
Journal ArticleDOI
The “Jekyll and Hyde” Actions of Nucleic Acids on the Prion-like Aggregation of Proteins
Jerson L. Silva,Yraima Cordeiro +1 more
TL;DR: How nucleic acid binding might influence protein misfolding for both disease-related and benign, functional prions and why the line between bad and good amyloids might be more subtle than previously thought are discussed.
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