Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2

An upregulation of NSD2, a histone H3 lysine 36 (H3K36) methyltransferase is linked to multiple myeloma and other types of cancer. Here, the authors provide insights into the regulatory mechanism of NSD2 by determining the 2.8 Å cryo-EM structure of the NSD2 bound nucleosome complex, and based on MD...

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Autores principales:	Ko Sato, Amarjeet Kumar, Keisuke Hamada, Chikako Okada, Asako Oguni, Ayumi Machiyama, Shun Sakuraba, Tomohiro Nishizawa, Osamu Nureki, Hidetoshi Kono, Kazuhiro Ogata, Toru Sengoku
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a236ab6e4fda4b94ae5feb9f8adae7d1
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spelling	oai:doaj.org-article:a236ab6e4fda4b94ae5feb9f8adae7d12021-11-21T12:35:40ZStructural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD210.1038/s41467-021-26913-52041-1723https://doaj.org/article/a236ab6e4fda4b94ae5feb9f8adae7d12021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26913-5https://doaj.org/toc/2041-1723An upregulation of NSD2, a histone H3 lysine 36 (H3K36) methyltransferase is linked to multiple myeloma and other types of cancer. Here, the authors provide insights into the regulatory mechanism of NSD2 by determining the 2.8 Å cryo-EM structure of the NSD2 bound nucleosome complex, and based on MD simulations they discuss how two oncogenic mutations enhance NSD2 activity.Ko SatoAmarjeet KumarKeisuke HamadaChikako OkadaAsako OguniAyumi MachiyamaShun SakurabaTomohiro NishizawaOsamu NurekiHidetoshi KonoKazuhiro OgataToru SengokuNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ko Sato Amarjeet Kumar Keisuke Hamada Chikako Okada Asako Oguni Ayumi Machiyama Shun Sakuraba Tomohiro Nishizawa Osamu Nureki Hidetoshi Kono Kazuhiro Ogata Toru Sengoku Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
description	An upregulation of NSD2, a histone H3 lysine 36 (H3K36) methyltransferase is linked to multiple myeloma and other types of cancer. Here, the authors provide insights into the regulatory mechanism of NSD2 by determining the 2.8 Å cryo-EM structure of the NSD2 bound nucleosome complex, and based on MD simulations they discuss how two oncogenic mutations enhance NSD2 activity.
format	article
author	Ko Sato Amarjeet Kumar Keisuke Hamada Chikako Okada Asako Oguni Ayumi Machiyama Shun Sakuraba Tomohiro Nishizawa Osamu Nureki Hidetoshi Kono Kazuhiro Ogata Toru Sengoku
author_facet	Ko Sato Amarjeet Kumar Keisuke Hamada Chikako Okada Asako Oguni Ayumi Machiyama Shun Sakuraba Tomohiro Nishizawa Osamu Nureki Hidetoshi Kono Kazuhiro Ogata Toru Sengoku
author_sort	Ko Sato
title	Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
title_short	Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
title_full	Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
title_fullStr	Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
title_full_unstemmed	Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
title_sort	structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone h3 lys36 by nsd2
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a236ab6e4fda4b94ae5feb9f8adae7d1
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Structural basis of the regulation of the normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2

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