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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eLife Sciences Publications Ltd
2015-08-01
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Series: | eLife |
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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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id | doaj.art-03029cfc861642f0a8ebbe642666889b |
institution | Directory Open Access Journal |
issn | 2050-084X |
language | English |
last_indexed | 2024-04-14T07:41:00Z |
publishDate | 2015-08-01 |
publisher | eLife Sciences Publications Ltd |
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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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