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Details

Autor(en) / Beteiligte
Titel
Phase separation of a yeast prion protein promotes cellular fitness
Ist Teil von
  • Science (American Association for the Advancement of Science), 2018-01, Vol.359 (6371)
Ort / Verlag
United States: The American Association for the Advancement of Science
Erscheinungsjahr
2018
Quelle
American Association for the Advancement of Science
Beschreibungen/Notizen
  • 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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