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

Ko Sato; Amarjeet Kumar; Keisuke Hamada; Chikako Okada; Asako Oguni; Ayumi Machiyama; Shun Sakuraba; Tomohiro Nishizawa; Osamu Nureki; Hidetoshi Kono; Kazuhiro Ogata; Toru Sengoku

doi:10.1038/s41467-021-26913-5

Nature Communications (Nov 2021)

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

Ko Sato,
Amarjeet Kumar,
Keisuke Hamada,
Chikako Okada,
Asako Oguni,
Ayumi Machiyama,
Shun Sakuraba,
Tomohiro Nishizawa,
Osamu Nureki,
Hidetoshi Kono,
Kazuhiro Ogata,
Toru Sengoku

Affiliations

Ko Sato: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Amarjeet Kumar: Institute for Quantum Life Science, National Institutes for Quantum Science and Technology
Keisuke Hamada: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Chikako Okada: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Asako Oguni: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Ayumi Machiyama: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Shun Sakuraba: Institute for Quantum Life Science, National Institutes for Quantum Science and Technology
Tomohiro Nishizawa: Department of Biological Sciences, Graduate School of Science, The University of Tokyo
Osamu Nureki: Department of Biological Sciences, Graduate School of Science, The University of Tokyo
Hidetoshi Kono: Institute for Quantum Life Science, National Institutes for Quantum Science and Technology
Kazuhiro Ogata: Department of Biochemistry, Yokohama City University Graduate School of Medicine
Toru Sengoku: Department of Biochemistry, Yokohama City University Graduate School of Medicine

DOI: https://doi.org/10.1038/s41467-021-26913-5
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 10

Abstract

Read online

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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal