Structural basis underlying viral hijacking of a histone chaperone complex

The Epstein-Barr virus tegument protein BNRF1 is required for the establishment of selective viral gene expression during latency and interacts with the histone chaperone DAXX. Here the authors provide structural insight into how BNRF1 hijacks the DAXX-histone H3.3-H4 complex.

Guardado en:

Detalles Bibliográficos
Autores principales:	Hongda Huang, Zhong Deng, Olga Vladimirova, Andreas Wiedmer, Fang Lu, Paul M. Lieberman, Dinshaw J. Patel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6d2925404a094e03b04d736dea4baa8d
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:6d2925404a094e03b04d736dea4baa8d
record_format	dspace
spelling	oai:doaj.org-article:6d2925404a094e03b04d736dea4baa8d2021-12-02T15:35:21ZStructural basis underlying viral hijacking of a histone chaperone complex10.1038/ncomms127072041-1723https://doaj.org/article/6d2925404a094e03b04d736dea4baa8d2016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12707https://doaj.org/toc/2041-1723The Epstein-Barr virus tegument protein BNRF1 is required for the establishment of selective viral gene expression during latency and interacts with the histone chaperone DAXX. Here the authors provide structural insight into how BNRF1 hijacks the DAXX-histone H3.3-H4 complex.Hongda HuangZhong DengOlga VladimirovaAndreas WiedmerFang LuPaul M. LiebermanDinshaw J. PatelNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hongda Huang Zhong Deng Olga Vladimirova Andreas Wiedmer Fang Lu Paul M. Lieberman Dinshaw J. Patel Structural basis underlying viral hijacking of a histone chaperone complex
description	The Epstein-Barr virus tegument protein BNRF1 is required for the establishment of selective viral gene expression during latency and interacts with the histone chaperone DAXX. Here the authors provide structural insight into how BNRF1 hijacks the DAXX-histone H3.3-H4 complex.
format	article
author	Hongda Huang Zhong Deng Olga Vladimirova Andreas Wiedmer Fang Lu Paul M. Lieberman Dinshaw J. Patel
author_facet	Hongda Huang Zhong Deng Olga Vladimirova Andreas Wiedmer Fang Lu Paul M. Lieberman Dinshaw J. Patel
author_sort	Hongda Huang
title	Structural basis underlying viral hijacking of a histone chaperone complex
title_short	Structural basis underlying viral hijacking of a histone chaperone complex
title_full	Structural basis underlying viral hijacking of a histone chaperone complex
title_fullStr	Structural basis underlying viral hijacking of a histone chaperone complex
title_full_unstemmed	Structural basis underlying viral hijacking of a histone chaperone complex
title_sort	structural basis underlying viral hijacking of a histone chaperone complex
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/6d2925404a094e03b04d736dea4baa8d
work_keys_str_mv	AT hongdahuang structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT zhongdeng structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT olgavladimirova structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT andreaswiedmer structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT fanglu structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT paulmlieberman structuralbasisunderlyingviralhijackingofahistonechaperonecomplex AT dinshawjpatel structuralbasisunderlyingviralhijackingofahistonechaperonecomplex
_version_	1718386602133159936

Structural basis underlying viral hijacking of a histone chaperone complex

Ejemplares similares