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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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Autores principales: Kroschwald, Sonja, Maharana, Shovamayee, Mateju, Daniel, Malinovska, Liliana, Nüske, Elisabeth, Poser, Ina, Richter, Doris, Alberti, Simon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4522596/
https://www.ncbi.nlm.nih.gov/pubmed/26238190
http://dx.doi.org/10.7554/eLife.06807
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author Kroschwald, Sonja
Maharana, Shovamayee
Mateju, Daniel
Malinovska, Liliana
Nüske, Elisabeth
Poser, Ina
Richter, Doris
Alberti, Simon
author_facet Kroschwald, Sonja
Maharana, Shovamayee
Mateju, Daniel
Malinovska, Liliana
Nüske, Elisabeth
Poser, Ina
Richter, Doris
Alberti, Simon
author_sort Kroschwald, Sonja
collection PubMed
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. DOI: http://dx.doi.org/10.7554/eLife.06807.001
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spelling pubmed-45225962015-08-05 Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules Kroschwald, Sonja Maharana, Shovamayee Mateju, Daniel Malinovska, Liliana Nüske, Elisabeth Poser, Ina Richter, Doris Alberti, Simon eLife Biochemistry 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. DOI: http://dx.doi.org/10.7554/eLife.06807.001 eLife Sciences Publications, Ltd 2015-08-04 /pmc/articles/PMC4522596/ /pubmed/26238190 http://dx.doi.org/10.7554/eLife.06807 Text en © 2015, Kroschwald et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry
Kroschwald, Sonja
Maharana, Shovamayee
Mateju, Daniel
Malinovska, Liliana
Nüske, Elisabeth
Poser, Ina
Richter, Doris
Alberti, Simon
Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
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 Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4522596/
https://www.ncbi.nlm.nih.gov/pubmed/26238190
http://dx.doi.org/10.7554/eLife.06807
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