Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4

MLL3 and MLL4 are members of the SET1/MLL family of histone H3K4 methyltransferases, which are responsible for monomethylating histone H3K4 on enhancers. Here the authors show that an extended PHD domain (ePHD6) in MLL3 and MLL4 specifically recognizes an H4H18-containing fragment of histone H4, and...

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Autores principales:	Yanli Liu, Su Qin, Tsai-Yu Chen, Ming Lei, Shilpa S. Dhar, Jolene Caifeng Ho, Aiping Dong, Peter Loppnau, Yanjun Li, Min Gyu Lee, Jinrong Min
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/dd25eb29a56b4175b0c7fc357946f2ae
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spelling	oai:doaj.org-article:dd25eb29a56b4175b0c7fc357946f2ae2021-12-02T14:39:17ZStructural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/410.1038/s41467-018-07906-32041-1723https://doaj.org/article/dd25eb29a56b4175b0c7fc357946f2ae2019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07906-3https://doaj.org/toc/2041-1723MLL3 and MLL4 are members of the SET1/MLL family of histone H3K4 methyltransferases, which are responsible for monomethylating histone H3K4 on enhancers. Here the authors show that an extended PHD domain (ePHD6) in MLL3 and MLL4 specifically recognizes an H4H18-containing fragment of histone H4, and that modifications of residues surrounding H4H18 modulate H4 binding to MLL3/4.Yanli LiuSu QinTsai-Yu ChenMing LeiShilpa S. DharJolene Caifeng HoAiping DongPeter LoppnauYanjun LiMin Gyu LeeJinrong MinNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yanli Liu Su Qin Tsai-Yu Chen Ming Lei Shilpa S. Dhar Jolene Caifeng Ho Aiping Dong Peter Loppnau Yanjun Li Min Gyu Lee Jinrong Min Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
description	MLL3 and MLL4 are members of the SET1/MLL family of histone H3K4 methyltransferases, which are responsible for monomethylating histone H3K4 on enhancers. Here the authors show that an extended PHD domain (ePHD6) in MLL3 and MLL4 specifically recognizes an H4H18-containing fragment of histone H4, and that modifications of residues surrounding H4H18 modulate H4 binding to MLL3/4.
format	article
author	Yanli Liu Su Qin Tsai-Yu Chen Ming Lei Shilpa S. Dhar Jolene Caifeng Ho Aiping Dong Peter Loppnau Yanjun Li Min Gyu Lee Jinrong Min
author_facet	Yanli Liu Su Qin Tsai-Yu Chen Ming Lei Shilpa S. Dhar Jolene Caifeng Ho Aiping Dong Peter Loppnau Yanjun Li Min Gyu Lee Jinrong Min
author_sort	Yanli Liu
title	Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
title_short	Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
title_full	Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
title_fullStr	Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
title_full_unstemmed	Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4
title_sort	structural insights into trans-histone regulation of h3k4 methylation by unique histone h4 binding of mll3/4
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/dd25eb29a56b4175b0c7fc357946f2ae
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Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4

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