Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients

Abstract Biomolecular condensates are liquid-like membraneless compartments that contribute to the spatiotemporal organization of proteins, RNA, and other biomolecules inside cells. Some membraneless compartments, such as nucleoli, are dispersed as different condensates that do not grow beyond a cer...

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Autores principales: Ignacio Sanchez-Burgos, Jerelle A. Joseph, Rosana Collepardo-Guevara, Jorge R. Espinosa
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/521a2f5926d8490f959614a9ad5e2782
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spelling oai:doaj.org-article:521a2f5926d8490f959614a9ad5e27822021-12-02T16:24:22ZSize conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients10.1038/s41598-021-94309-y2045-2322https://doaj.org/article/521a2f5926d8490f959614a9ad5e27822021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-94309-yhttps://doaj.org/toc/2045-2322Abstract Biomolecular condensates are liquid-like membraneless compartments that contribute to the spatiotemporal organization of proteins, RNA, and other biomolecules inside cells. Some membraneless compartments, such as nucleoli, are dispersed as different condensates that do not grow beyond a certain size, or do not present coalescence over time. In this work, using a minimal protein model, we show that phase separation of binary mixtures of scaffolds and low-valency clients that can act as surfactants—i.e., that significantly reduce the droplet surface tension—can yield either a single drop or multiple droplets that conserve their sizes on long timescales (herein ‘multidroplet size-conserved’ scenario’), depending on the scaffold to client ratio. Our simulations demonstrate that protein connectivity and condensate surface tension regulate the balance between these two scenarios. The multidroplet size-conserved scenario spontaneously arises at increasing surfactant-to-scaffold concentrations, when the interfacial penalty for creating small liquid droplets is sufficiently reduced by the surfactant proteins that are preferentially located at the interface. In contrast, low surfactant-to-scaffold concentrations enable continuous growth and fusion of droplets without restrictions. Overall, our work proposes one thermodynamic mechanism to help rationalize how size-conserved coexisting condensates can persist inside cells—shedding light on the roles of protein connectivity, binding affinity, and droplet composition in this process.Ignacio Sanchez-BurgosJerelle A. JosephRosana Collepardo-GuevaraJorge R. EspinosaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Ignacio Sanchez-Burgos
Jerelle A. Joseph
Rosana Collepardo-Guevara
Jorge R. Espinosa
Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
description Abstract Biomolecular condensates are liquid-like membraneless compartments that contribute to the spatiotemporal organization of proteins, RNA, and other biomolecules inside cells. Some membraneless compartments, such as nucleoli, are dispersed as different condensates that do not grow beyond a certain size, or do not present coalescence over time. In this work, using a minimal protein model, we show that phase separation of binary mixtures of scaffolds and low-valency clients that can act as surfactants—i.e., that significantly reduce the droplet surface tension—can yield either a single drop or multiple droplets that conserve their sizes on long timescales (herein ‘multidroplet size-conserved’ scenario’), depending on the scaffold to client ratio. Our simulations demonstrate that protein connectivity and condensate surface tension regulate the balance between these two scenarios. The multidroplet size-conserved scenario spontaneously arises at increasing surfactant-to-scaffold concentrations, when the interfacial penalty for creating small liquid droplets is sufficiently reduced by the surfactant proteins that are preferentially located at the interface. In contrast, low surfactant-to-scaffold concentrations enable continuous growth and fusion of droplets without restrictions. Overall, our work proposes one thermodynamic mechanism to help rationalize how size-conserved coexisting condensates can persist inside cells—shedding light on the roles of protein connectivity, binding affinity, and droplet composition in this process.
format article
author Ignacio Sanchez-Burgos
Jerelle A. Joseph
Rosana Collepardo-Guevara
Jorge R. Espinosa
author_facet Ignacio Sanchez-Burgos
Jerelle A. Joseph
Rosana Collepardo-Guevara
Jorge R. Espinosa
author_sort Ignacio Sanchez-Burgos
title Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
title_short Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
title_full Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
title_fullStr Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
title_full_unstemmed Size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
title_sort size conservation emerges spontaneously in biomolecular condensates formed by scaffolds and surfactant clients
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/521a2f5926d8490f959614a9ad5e2782
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AT rosanacollepardoguevara sizeconservationemergesspontaneouslyinbiomolecularcondensatesformedbyscaffoldsandsurfactantclients
AT jorgerespinosa sizeconservationemergesspontaneouslyinbiomolecularcondensatesformedbyscaffoldsandsurfactantclients
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