Cryo-EM structure of the human MLL1 core complex bound to the nucleosome

MLL family histone methyltransferases deposit histone H3 Lys4 mono-/di-/tri-methylation and regulate gene expression in mammals. Here the authors report the single-particle cryo-EM structure of the NCP-bound human MLL1 core complex, shedding light on how the MLL1 complex engages chromatin and how ch...

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Autores principales:	Sang Ho Park, Alex Ayoub, Young-Tae Lee, Jing Xu, Hanseong Kim, Wei Zheng, Biao Zhang, Liang Sha, Sojin An, Yang Zhang, Michael A. Cianfrocco, Min Su, Yali Dou, Uhn-Soo Cho
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/dd454636ec51441b92111ea64c0ddfb1
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spelling	oai:doaj.org-article:dd454636ec51441b92111ea64c0ddfb12021-12-02T16:57:52ZCryo-EM structure of the human MLL1 core complex bound to the nucleosome10.1038/s41467-019-13550-22041-1723https://doaj.org/article/dd454636ec51441b92111ea64c0ddfb12019-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13550-2https://doaj.org/toc/2041-1723MLL family histone methyltransferases deposit histone H3 Lys4 mono-/di-/tri-methylation and regulate gene expression in mammals. Here the authors report the single-particle cryo-EM structure of the NCP-bound human MLL1 core complex, shedding light on how the MLL1 complex engages chromatin and how chromatin binding promotes MLL1 tri-methylation activity.Sang Ho ParkAlex AyoubYoung-Tae LeeJing XuHanseong KimWei ZhengBiao ZhangLiang ShaSojin AnYang ZhangMichael A. CianfroccoMin SuYali DouUhn-Soo ChoNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sang Ho Park Alex Ayoub Young-Tae Lee Jing Xu Hanseong Kim Wei Zheng Biao Zhang Liang Sha Sojin An Yang Zhang Michael A. Cianfrocco Min Su Yali Dou Uhn-Soo Cho Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
description	MLL family histone methyltransferases deposit histone H3 Lys4 mono-/di-/tri-methylation and regulate gene expression in mammals. Here the authors report the single-particle cryo-EM structure of the NCP-bound human MLL1 core complex, shedding light on how the MLL1 complex engages chromatin and how chromatin binding promotes MLL1 tri-methylation activity.
format	article
author	Sang Ho Park Alex Ayoub Young-Tae Lee Jing Xu Hanseong Kim Wei Zheng Biao Zhang Liang Sha Sojin An Yang Zhang Michael A. Cianfrocco Min Su Yali Dou Uhn-Soo Cho
author_facet	Sang Ho Park Alex Ayoub Young-Tae Lee Jing Xu Hanseong Kim Wei Zheng Biao Zhang Liang Sha Sojin An Yang Zhang Michael A. Cianfrocco Min Su Yali Dou Uhn-Soo Cho
author_sort	Sang Ho Park
title	Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
title_short	Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
title_full	Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
title_fullStr	Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
title_full_unstemmed	Cryo-EM structure of the human MLL1 core complex bound to the nucleosome
title_sort	cryo-em structure of the human mll1 core complex bound to the nucleosome
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/dd454636ec51441b92111ea64c0ddfb1
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Cryo-EM structure of the human MLL1 core complex bound to the nucleosome

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