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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Main Authors: Ko Sato, Amarjeet Kumar, Keisuke Hamada, Chikako Okada, Asako Oguni, Ayumi Machiyama, Shun Sakuraba, Tomohiro Nishizawa, Osamu Nureki, Hidetoshi Kono, Kazuhiro Ogata, Toru Sengoku
Format: article
Language:EN
Published: Nature Portfolio 2021
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Online Access:https://doaj.org/article/a236ab6e4fda4b94ae5feb9f8adae7d1
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Summary: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.