期刊
SCIENCE
卷 359, 期 6371, 页码 47-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao5654
关键词
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资金
- Services and Facilities of the Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG)
- German Federal Ministry of Research and Education [BMBF 031A359A]
- MaxSynBio consortium
- Federal Ministry of Education and Research of Germany
- Max Planck Society
- U.S. National Institutes of Health [5RO1NS056114]
- Human Frontiers Program [RGP0034/2017]
- Volkswagen Life? initiative
- German Research Foundation (DFG)
Despite the important role of prion domains in neurodegenerative disease, their physiological function has remained enigmatic. Previous work with yeast prions has defined prion domains as sequences that form self-propagating aggregates. Here, we uncovered an unexpected function of the canonical yeast prion protein Sup35. In stressed conditions, Sup35 formed protective gels via pH-regulated liquid-like phase separation followed by gelation. Phase separation was mediated by the N-terminal prion domain and regulated by the adjacent pH sensor domain. Phase separation promoted yeast cell survival by rescuing the essential Sup35 translation factor from stress-induced damage. Thus, prion-like domains represent conserved environmental stress sensors that facilitate rapid adaptation in unstable environments by modifying protein phase behavior.
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