Structural Bases of Prion Variation in Yeast.

Autor: Kushnirov VV; A.N. Bach Institute of Biochemistry, Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Moscow 119071, Russia., Dergalev AA; A.N. Bach Institute of Biochemistry, Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Moscow 119071, Russia., Alieva MK; A.N. Bach Institute of Biochemistry, Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Moscow 119071, Russia., Alexandrov AI; A.N. Bach Institute of Biochemistry, Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Moscow 119071, Russia.
Jazyk: angličtina
Zdroj: International journal of molecular sciences [Int J Mol Sci] 2022 May 20; Vol. 23 (10). Date of Electronic Publication: 2022 May 20.
DOI: 10.3390/ijms23105738
Abstrakt: 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.
Databáze: MEDLINE
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