Osmotic stress induces formation of both liquid condensates and amyloids by a yeast prion domain.

Autor:	Grizel AV; School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia, USA., Gorsheneva NA; Laboratory of Amyloid Biology and Department of Genetics and Biotechnology, St Petersburg State University, St Petersburg, Russia., Stevenson JB; School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia, USA., Pflaum J; Mechanisms of Cellular Quality Control, Max Planck Institute of Biophysics, Frankfurt, Germany., Wilfling F; Mechanisms of Cellular Quality Control, Max Planck Institute of Biophysics, Frankfurt, Germany., Rubel AA; Laboratory of Amyloid Biology and Department of Genetics and Biotechnology, St Petersburg State University, St Petersburg, Russia., Chernoff YO; School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia, USA. Electronic address: yury.chernoff@biology.gatech.edu.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2024 Oct; Vol. 300 (10), pp. 107766. Date of Electronic Publication: 2024 Sep 12.
DOI:	10.1016/j.jbc.2024.107766
Abstrakt:	Liquid protein condensates produced by phase separation are involved in the spatiotemporal control of cellular functions, while solid fibrous aggregates (amyloids) are associated with diseases and/or manifest as infectious or heritable elements (prions). Relationships between these assemblies are poorly understood. The Saccharomyces cerevisiae release factor Sup35 can produce both fluid liquid-like condensates (e.g., at acidic pH) and amyloids (typically cross-seeded by other prions). We observed acidification-independent formation of Sup35-based liquid condensates in response to hyperosmotic shock in the absence of other prions, both at increased and physiological expression levels. The Sup35 prion domain, Sup35N, is both necessary and sufficient for condensate formation, while the middle domain, Sup35M antagonizes this process. Formation of liquid condensates in response to osmotic stress is conserved within yeast evolution. Notably, condensates of Sup35N/NM protein originated from the distantly related yeast Ogataea methanolica can directly convert to amyloids in osmotically stressed S. cerevisiae cells, providing a unique opportunity for real-time monitoring of condensate-to-fibril transition in vivo by fluorescence microscopy. Thus, cellular fate of stress-induced condensates depends on protein properties and/or intracellular environment. Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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