Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release

The histone chaperone nucleoplasmin (Npm) stores histones H2A/H2B in the egg and embryo. Here, the authors use NMR to show that Npm’s intrinsically disordered tail domain controls histone binding at an acidic stretch, which is autoregulated through direct competition with its basic C-terminus.

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Autores principales:	Christopher Warren, Tsutomu Matsui, Jerome M. Karp, Takashi Onikubo, Sean Cahill, Michael Brenowitz, David Cowburn, Mark Girvin, David Shechter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f49d4636918c4df182e86b219d111626
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spelling	oai:doaj.org-article:f49d4636918c4df182e86b219d1116262021-12-02T17:06:16ZDynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release10.1038/s41467-017-02308-32041-1723https://doaj.org/article/f49d4636918c4df182e86b219d1116262017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02308-3https://doaj.org/toc/2041-1723The histone chaperone nucleoplasmin (Npm) stores histones H2A/H2B in the egg and embryo. Here, the authors use NMR to show that Npm’s intrinsically disordered tail domain controls histone binding at an acidic stretch, which is autoregulated through direct competition with its basic C-terminus.Christopher WarrenTsutomu MatsuiJerome M. KarpTakashi OnikuboSean CahillMichael BrenowitzDavid CowburnMark GirvinDavid ShechterNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Christopher Warren Tsutomu Matsui Jerome M. Karp Takashi Onikubo Sean Cahill Michael Brenowitz David Cowburn Mark Girvin David Shechter Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
description	The histone chaperone nucleoplasmin (Npm) stores histones H2A/H2B in the egg and embryo. Here, the authors use NMR to show that Npm’s intrinsically disordered tail domain controls histone binding at an acidic stretch, which is autoregulated through direct competition with its basic C-terminus.
format	article
author	Christopher Warren Tsutomu Matsui Jerome M. Karp Takashi Onikubo Sean Cahill Michael Brenowitz David Cowburn Mark Girvin David Shechter
author_facet	Christopher Warren Tsutomu Matsui Jerome M. Karp Takashi Onikubo Sean Cahill Michael Brenowitz David Cowburn Mark Girvin David Shechter
author_sort	Christopher Warren
title	Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
title_short	Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
title_full	Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
title_fullStr	Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
title_full_unstemmed	Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
title_sort	dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f49d4636918c4df182e86b219d111626
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Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release

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