Structural Bases of Prion Variation in Yeast

Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of inter...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-05, Vol.23 (10), p.5738
Main Authors: Kushnirov, Vitaly V, Dergalev, Alexander A, Alieva, Maya K, Alexandrov, Alexander I
Format: Article
Language:English
Subjects:
Amyloid
chaperones
Insects
Polypeptides
prion
Prion protein
prion structure
Prions
Proteins
Review
Sup35
Yeast
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Summary:Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23105738