Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

Regulation of the MLL family of histone H3K4 methyltransferases on the nucleosome core particle (NCP) remains largely unknown. Here the authors show that intrinsically disordered regions of ASH2L and DPY30 restrict the rotational dynamics of MLL1 on the NCP, allowing more efficient enzyme-substrate...

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Autores principales:	Young-Tae Lee, Alex Ayoub, Sang-Ho Park, Liang Sha, Jing Xu, Fengbiao Mao, Wei Zheng, Yang Zhang, Uhn-Soo Cho, Yali Dou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/579dbc95fb704acb953fca9b4d33ed4c
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id	oai:doaj.org-article:579dbc95fb704acb953fca9b4d33ed4c
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spelling	oai:doaj.org-article:579dbc95fb704acb953fca9b4d33ed4c2021-12-02T15:45:24ZMechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin10.1038/s41467-021-23268-92041-1723https://doaj.org/article/579dbc95fb704acb953fca9b4d33ed4c2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23268-9https://doaj.org/toc/2041-1723Regulation of the MLL family of histone H3K4 methyltransferases on the nucleosome core particle (NCP) remains largely unknown. Here the authors show that intrinsically disordered regions of ASH2L and DPY30 restrict the rotational dynamics of MLL1 on the NCP, allowing more efficient enzyme-substrate engagement and higher H3K4 trimethylation activity.Young-Tae LeeAlex AyoubSang-Ho ParkLiang ShaJing XuFengbiao MaoWei ZhengYang ZhangUhn-Soo ChoYali DouNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Young-Tae Lee Alex Ayoub Sang-Ho Park Liang Sha Jing Xu Fengbiao Mao Wei Zheng Yang Zhang Uhn-Soo Cho Yali Dou Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
description	Regulation of the MLL family of histone H3K4 methyltransferases on the nucleosome core particle (NCP) remains largely unknown. Here the authors show that intrinsically disordered regions of ASH2L and DPY30 restrict the rotational dynamics of MLL1 on the NCP, allowing more efficient enzyme-substrate engagement and higher H3K4 trimethylation activity.
format	article
author	Young-Tae Lee Alex Ayoub Sang-Ho Park Liang Sha Jing Xu Fengbiao Mao Wei Zheng Yang Zhang Uhn-Soo Cho Yali Dou
author_facet	Young-Tae Lee Alex Ayoub Sang-Ho Park Liang Sha Jing Xu Fengbiao Mao Wei Zheng Yang Zhang Uhn-Soo Cho Yali Dou
author_sort	Young-Tae Lee
title	Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
title_short	Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
title_full	Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
title_fullStr	Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
title_full_unstemmed	Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin
title_sort	mechanism for dpy30 and ash2l intrinsically disordered regions to modulate the mll/set1 activity on chromatin
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/579dbc95fb704acb953fca9b4d33ed4c
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Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

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