Lysine/RNA-interactions drive and regulate biomolecular condensation

Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dyna...

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Autores principales:	Tina Ukmar-Godec, Saskia Hutten, Matthew P. Grieshop, Nasrollah Rezaei-Ghaleh, Maria-Sol Cima-Omori, Jacek Biernat, Eckhard Mandelkow, Johannes Söding, Dorothee Dormann, Markus Zweckstetter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ba5821511fba49e2bd2ace00270992df
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spelling	oai:doaj.org-article:ba5821511fba49e2bd2ace00270992df2021-12-02T16:57:21ZLysine/RNA-interactions drive and regulate biomolecular condensation10.1038/s41467-019-10792-y2041-1723https://doaj.org/article/ba5821511fba49e2bd2ace00270992df2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10792-yhttps://doaj.org/toc/2041-1723Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dynamic lysine/RNA-coacervates and lysine acetylation reverses liquid-liquid phase separation.Tina Ukmar-GodecSaskia HuttenMatthew P. GrieshopNasrollah Rezaei-GhalehMaria-Sol Cima-OmoriJacek BiernatEckhard MandelkowJohannes SödingDorothee DormannMarkus ZweckstetterNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tina Ukmar-Godec Saskia Hutten Matthew P. Grieshop Nasrollah Rezaei-Ghaleh Maria-Sol Cima-Omori Jacek Biernat Eckhard Mandelkow Johannes Söding Dorothee Dormann Markus Zweckstetter Lysine/RNA-interactions drive and regulate biomolecular condensation
description	Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dynamic lysine/RNA-coacervates and lysine acetylation reverses liquid-liquid phase separation.
format	article
author	Tina Ukmar-Godec Saskia Hutten Matthew P. Grieshop Nasrollah Rezaei-Ghaleh Maria-Sol Cima-Omori Jacek Biernat Eckhard Mandelkow Johannes Söding Dorothee Dormann Markus Zweckstetter
author_facet	Tina Ukmar-Godec Saskia Hutten Matthew P. Grieshop Nasrollah Rezaei-Ghaleh Maria-Sol Cima-Omori Jacek Biernat Eckhard Mandelkow Johannes Söding Dorothee Dormann Markus Zweckstetter
author_sort	Tina Ukmar-Godec
title	Lysine/RNA-interactions drive and regulate biomolecular condensation
title_short	Lysine/RNA-interactions drive and regulate biomolecular condensation
title_full	Lysine/RNA-interactions drive and regulate biomolecular condensation
title_fullStr	Lysine/RNA-interactions drive and regulate biomolecular condensation
title_full_unstemmed	Lysine/RNA-interactions drive and regulate biomolecular condensation
title_sort	lysine/rna-interactions drive and regulate biomolecular condensation
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/ba5821511fba49e2bd2ace00270992df
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Lysine/RNA-interactions drive and regulate biomolecular condensation

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