Structural basis of specific H2A K13/K15 ubiquitination by RNF168

Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13...

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Autores principales:	Velten Horn, Michael Uckelmann, Heyi Zhang, Jelmer Eerland, Ivette Aarsman, Ulric B. le Paige, Chen Davidovich, Titia K. Sixma, Hugo van Ingen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3e125f2b63794fa29d89db5f5520deba
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spelling	oai:doaj.org-article:3e125f2b63794fa29d89db5f5520deba2021-12-02T16:57:34ZStructural basis of specific H2A K13/K15 ubiquitination by RNF16810.1038/s41467-019-09756-z2041-1723https://doaj.org/article/3e125f2b63794fa29d89db5f5520deba2019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09756-zhttps://doaj.org/toc/2041-1723Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13/K15.Velten HornMichael UckelmannHeyi ZhangJelmer EerlandIvette AarsmanUlric B. le PaigeChen DavidovichTitia K. SixmaHugo van IngenNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Velten Horn Michael Uckelmann Heyi Zhang Jelmer Eerland Ivette Aarsman Ulric B. le Paige Chen Davidovich Titia K. Sixma Hugo van Ingen Structural basis of specific H2A K13/K15 ubiquitination by RNF168
description	Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13/K15.
format	article
author	Velten Horn Michael Uckelmann Heyi Zhang Jelmer Eerland Ivette Aarsman Ulric B. le Paige Chen Davidovich Titia K. Sixma Hugo van Ingen
author_facet	Velten Horn Michael Uckelmann Heyi Zhang Jelmer Eerland Ivette Aarsman Ulric B. le Paige Chen Davidovich Titia K. Sixma Hugo van Ingen
author_sort	Velten Horn
title	Structural basis of specific H2A K13/K15 ubiquitination by RNF168
title_short	Structural basis of specific H2A K13/K15 ubiquitination by RNF168
title_full	Structural basis of specific H2A K13/K15 ubiquitination by RNF168
title_fullStr	Structural basis of specific H2A K13/K15 ubiquitination by RNF168
title_full_unstemmed	Structural basis of specific H2A K13/K15 ubiquitination by RNF168
title_sort	structural basis of specific h2a k13/k15 ubiquitination by rnf168
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/3e125f2b63794fa29d89db5f5520deba
work_keys_str_mv	AT veltenhorn structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT michaeluckelmann structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT heyizhang structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT jelmereerland structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT ivetteaarsman structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT ulricblepaige structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT chendavidovich structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT titiaksixma structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168 AT hugovaningen structuralbasisofspecifich2ak13k15ubiquitinationbyrnf168
_version_	1718382496495697920

Structural basis of specific H2A K13/K15 ubiquitination by RNF168

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