A multi-step nucleation process determines the kinetics of prion-like domain phase separation

The nucleation mechanisms of biological protein phase separation are poorly understood. Here, the authors perform time-resolved SAXS experiments with the low-complexity domain (LCD) of hnRNPA1 and uncover multiple kinetic regimes on the micro- to millisecond timescale. Initially, individual proteins...

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Autores principales:	Erik W. Martin, Tyler S. Harmon, Jesse B. Hopkins, Srinivas Chakravarthy, J. Jeremías Incicco, Peter Schuck, Andrea Soranno, Tanja Mittag
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3515d63866274f01b905879042d061a9
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spelling	oai:doaj.org-article:3515d63866274f01b905879042d061a92021-12-02T17:57:04ZA multi-step nucleation process determines the kinetics of prion-like domain phase separation10.1038/s41467-021-24727-z2041-1723https://doaj.org/article/3515d63866274f01b905879042d061a92021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24727-zhttps://doaj.org/toc/2041-1723The nucleation mechanisms of biological protein phase separation are poorly understood. Here, the authors perform time-resolved SAXS experiments with the low-complexity domain (LCD) of hnRNPA1 and uncover multiple kinetic regimes on the micro- to millisecond timescale. Initially, individual proteins collapse. Nucleation then occurs via two steps distinguished by their protein cluster size distributions.Erik W. MartinTyler S. HarmonJesse B. HopkinsSrinivas ChakravarthyJ. Jeremías InciccoPeter SchuckAndrea SorannoTanja MittagNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Erik W. Martin Tyler S. Harmon Jesse B. Hopkins Srinivas Chakravarthy J. Jeremías Incicco Peter Schuck Andrea Soranno Tanja Mittag A multi-step nucleation process determines the kinetics of prion-like domain phase separation
description	The nucleation mechanisms of biological protein phase separation are poorly understood. Here, the authors perform time-resolved SAXS experiments with the low-complexity domain (LCD) of hnRNPA1 and uncover multiple kinetic regimes on the micro- to millisecond timescale. Initially, individual proteins collapse. Nucleation then occurs via two steps distinguished by their protein cluster size distributions.
format	article
author	Erik W. Martin Tyler S. Harmon Jesse B. Hopkins Srinivas Chakravarthy J. Jeremías Incicco Peter Schuck Andrea Soranno Tanja Mittag
author_facet	Erik W. Martin Tyler S. Harmon Jesse B. Hopkins Srinivas Chakravarthy J. Jeremías Incicco Peter Schuck Andrea Soranno Tanja Mittag
author_sort	Erik W. Martin
title	A multi-step nucleation process determines the kinetics of prion-like domain phase separation
title_short	A multi-step nucleation process determines the kinetics of prion-like domain phase separation
title_full	A multi-step nucleation process determines the kinetics of prion-like domain phase separation
title_fullStr	A multi-step nucleation process determines the kinetics of prion-like domain phase separation
title_full_unstemmed	A multi-step nucleation process determines the kinetics of prion-like domain phase separation
title_sort	multi-step nucleation process determines the kinetics of prion-like domain phase separation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/3515d63866274f01b905879042d061a9
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A multi-step nucleation process determines the kinetics of prion-like domain phase separation

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