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RNA-binding and prion domains: the Yin and Yang of phase separation

Proteins and RNAs assemble in membrane-less organelles that organize intracellular spaces and regulate biochemical reactions. The ability of proteins and RNAs to form condensates is encoded in their sequences, yet it is unknown which domains drive the phase separation (PS) process and what are their...

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Autores principales: Gotor, Nieves Lorenzo, Armaos, Alexandros, Calloni, Giulia, Torrent Burgas, Marc, Vabulas, R Martin, De Groot, Natalia Sanchez, Tartaglia, Gian Gaetano
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7515694/
https://www.ncbi.nlm.nih.gov/pubmed/32857852
http://dx.doi.org/10.1093/nar/gkaa681
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author Gotor, Nieves Lorenzo
Armaos, Alexandros
Calloni, Giulia
Torrent Burgas, Marc
Vabulas, R Martin
De Groot, Natalia Sanchez
Tartaglia, Gian Gaetano
author_facet Gotor, Nieves Lorenzo
Armaos, Alexandros
Calloni, Giulia
Torrent Burgas, Marc
Vabulas, R Martin
De Groot, Natalia Sanchez
Tartaglia, Gian Gaetano
author_sort Gotor, Nieves Lorenzo
collection PubMed
description Proteins and RNAs assemble in membrane-less organelles that organize intracellular spaces and regulate biochemical reactions. The ability of proteins and RNAs to form condensates is encoded in their sequences, yet it is unknown which domains drive the phase separation (PS) process and what are their specific roles. Here, we systematically investigated the human and yeast proteomes to find regions promoting condensation. Using advanced computational methods to predict the PS propensity of proteins, we designed a set of experiments to investigate the contributions of Prion-Like Domains (PrLDs) and RNA-binding domains (RBDs). We found that one PrLD is sufficient to drive PS, whereas multiple RBDs are needed to modulate the dynamics of the assemblies. In the case of stress granule protein Pub1 we show that the PrLD promotes sequestration of protein partners and the RBD confers liquid-like behaviour to the condensate. Our work sheds light on the fine interplay between RBDs and PrLD to regulate formation of membrane-less organelles, opening up the avenue for their manipulation.
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spelling pubmed-75156942020-09-30 RNA-binding and prion domains: the Yin and Yang of phase separation Gotor, Nieves Lorenzo Armaos, Alexandros Calloni, Giulia Torrent Burgas, Marc Vabulas, R Martin De Groot, Natalia Sanchez Tartaglia, Gian Gaetano Nucleic Acids Res Computational Biology Proteins and RNAs assemble in membrane-less organelles that organize intracellular spaces and regulate biochemical reactions. The ability of proteins and RNAs to form condensates is encoded in their sequences, yet it is unknown which domains drive the phase separation (PS) process and what are their specific roles. Here, we systematically investigated the human and yeast proteomes to find regions promoting condensation. Using advanced computational methods to predict the PS propensity of proteins, we designed a set of experiments to investigate the contributions of Prion-Like Domains (PrLDs) and RNA-binding domains (RBDs). We found that one PrLD is sufficient to drive PS, whereas multiple RBDs are needed to modulate the dynamics of the assemblies. In the case of stress granule protein Pub1 we show that the PrLD promotes sequestration of protein partners and the RBD confers liquid-like behaviour to the condensate. Our work sheds light on the fine interplay between RBDs and PrLD to regulate formation of membrane-less organelles, opening up the avenue for their manipulation. Oxford University Press 2020-08-28 /pmc/articles/PMC7515694/ /pubmed/32857852 http://dx.doi.org/10.1093/nar/gkaa681 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Computational Biology
Gotor, Nieves Lorenzo
Armaos, Alexandros
Calloni, Giulia
Torrent Burgas, Marc
Vabulas, R Martin
De Groot, Natalia Sanchez
Tartaglia, Gian Gaetano
RNA-binding and prion domains: the Yin and Yang of phase separation
title RNA-binding and prion domains: the Yin and Yang of phase separation
title_full RNA-binding and prion domains: the Yin and Yang of phase separation
title_fullStr RNA-binding and prion domains: the Yin and Yang of phase separation
title_full_unstemmed RNA-binding and prion domains: the Yin and Yang of phase separation
title_short RNA-binding and prion domains: the Yin and Yang of phase separation
title_sort rna-binding and prion domains: the yin and yang of phase separation
topic Computational Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7515694/
https://www.ncbi.nlm.nih.gov/pubmed/32857852
http://dx.doi.org/10.1093/nar/gkaa681
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