Methylation of Histone H3K79 by Dot1L Requires Multiple Contacts with the Ubiquitinated Nucleosome

Yi Zhang; Tatiana G Kutateladze

doi:10.1016/j.molcel.2019.05.013

Methylation of Histone H3K79 by Dot1L Requires Multiple Contacts with the Ubiquitinated Nucleosome

Mol Cell. 2019 Jun 6;74(5):862-863. doi: 10.1016/j.molcel.2019.05.013.

Authors

Yi Zhang¹, Tatiana G Kutateladze²

Affiliations

¹ Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
² Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA. Electronic address: tatiana.kutateladze@ucdenver.edu.

PMID: 31173720
DOI: 10.1016/j.molcel.2019.05.013

Abstract

Cryo-EM structures of Dot1L in complex with a ubiquitinated nucleosome provide the long-sought-after molecular mechanism of Dot1L-mediated methylation of lysine 79 in histone H3 and explain crosstalk with histone H2B ubiquitination.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Histones*
Lysine
Methylation
Methyltransferases / genetics
Nucleosomes*
Ubiquitination

Substances

Histones
Nucleosomes
Methyltransferases
Lysine