Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules

RNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid RNA/protein phase. Which model describes RNP granules in living cells is still unclear. In this study, we analyze P bodies in budding yeast and find that they h...

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Main Authors: Sonja Kroschwald, Shovamayee Maharana, Daniel Mateju, Liliana Malinovska, Elisabeth Nüske, Ina Poser, Doris Richter, Simon Alberti
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2015-08-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/06807
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author Sonja Kroschwald
Shovamayee Maharana
Daniel Mateju
Liliana Malinovska
Elisabeth Nüske
Ina Poser
Doris Richter
Simon Alberti
author_facet Sonja Kroschwald
Shovamayee Maharana
Daniel Mateju
Liliana Malinovska
Elisabeth Nüske
Ina Poser
Doris Richter
Simon Alberti
author_sort Sonja Kroschwald
collection DOAJ
description RNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid RNA/protein phase. Which model describes RNP granules in living cells is still unclear. In this study, we analyze P bodies in budding yeast and find that they have liquid-like properties. Surprisingly, yeast stress granules adopt a different material state, which is reminiscent of solid protein aggregates and controlled by protein disaggregases. By using an assay to ectopically nucleate RNP granules, we further establish that RNP granule formation does not depend on amyloid-like aggregation but rather involves many promiscuous interactions. Finally, we show that stress granules have different properties in mammalian cells, where they show liquid-like behavior. Thus, we propose that the material state of RNP granules is flexible and that the solid state of yeast stress granules is an adaptation to extreme environments, made possible by the presence of a powerful disaggregation machine.
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spelling doaj.art-03029cfc861642f0a8ebbe642666889b2022-12-22T02:05:30ZengeLife Sciences Publications LtdeLife2050-084X2015-08-01410.7554/eLife.06807Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granulesSonja Kroschwald0Shovamayee Maharana1Daniel Mateju2Liliana Malinovska3Elisabeth Nüske4Ina Poser5Doris Richter6Simon Alberti7Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, GermanyRNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid RNA/protein phase. Which model describes RNP granules in living cells is still unclear. In this study, we analyze P bodies in budding yeast and find that they have liquid-like properties. Surprisingly, yeast stress granules adopt a different material state, which is reminiscent of solid protein aggregates and controlled by protein disaggregases. By using an assay to ectopically nucleate RNP granules, we further establish that RNP granule formation does not depend on amyloid-like aggregation but rather involves many promiscuous interactions. Finally, we show that stress granules have different properties in mammalian cells, where they show liquid-like behavior. Thus, we propose that the material state of RNP granules is flexible and that the solid state of yeast stress granules is an adaptation to extreme environments, made possible by the presence of a powerful disaggregation machine.https://elifesciences.org/articles/06807phase separationprotein aggregationchaperoneprion-like proteinP bodystress granule
spellingShingle Sonja Kroschwald
Shovamayee Maharana
Daniel Mateju
Liliana Malinovska
Elisabeth Nüske
Ina Poser
Doris Richter
Simon Alberti
Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
eLife
phase separation
protein aggregation
chaperone
prion-like protein
P body
stress granule
title Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
title_full Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
title_fullStr Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
title_full_unstemmed Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
title_short Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
title_sort promiscuous interactions and protein disaggregases determine the material state of stress inducible rnp granules
topic phase separation
protein aggregation
chaperone
prion-like protein
P body
stress granule
url https://elifesciences.org/articles/06807
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