Phase separation of a yeast prion protein promotes cellular fitness.

Franzmann, Titus; Jahnel, Marcus; Pozniakovsky, Andrei I.; Mahamid, Julia; Holehouse, Alex S; Nüske, Elisabeth; Richter, Doris; Baumeister, Wolfgang; Grill, Stephan W.; Pappu, Rohit V; Hyman, Anthony A.; Alberti, Simon

doi:10.1126/science.aao5654

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Phase separation of a yeast prion protein promotes cellular fitness.

MPG-Autoren

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Franzmann, Titus
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Jahnel, Marcus
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Pozniakovsky, Andrei I.
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Mahamid, Julia
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219498

Nüske, Elisabeth
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Richter, Doris
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons145692

Grill, Stephan W.
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons219253

Hyman, Anthony A.
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Alberti, Simon
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Zitation

Franzmann, T., Jahnel, M., Pozniakovsky, A. I., Mahamid, J., Holehouse, A. S., Nüske, E., et al. (2018). Phase separation of a yeast prion protein promotes cellular fitness. Science (New York, N.Y.), 359(6371): eaao5654. doi:10.1126/science.aao5654.

Zitierlink: https://hdl.handle.net/21.11116/0000-0003-F5E7-4

Zusammenfassung

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.