Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation

Linjiao Zhou; Matthew T. Holt; Nami Ohashi; Aishan Zhao; Manuel M. Müller; Boyuan Wang; Tom W. Muir

doi:10.1038/ncomms10589

Nature Communications (Feb 2016)

Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation

Linjiao Zhou,
Matthew T. Holt,
Nami Ohashi,
Aishan Zhao,
Manuel M. Müller,
Boyuan Wang,
Tom W. Muir

Affiliations

Linjiao Zhou: Department of Chemistry, Princeton University
Matthew T. Holt: Laboratory of Synthetic Protein Chemistry, The Rockefeller University
Nami Ohashi: Department of Chemistry, Princeton University
Aishan Zhao: Department of Chemistry, Princeton University
Manuel M. Müller: Department of Chemistry, Princeton University
Boyuan Wang: Department of Chemistry, Princeton University
Tom W. Muir: Department of Chemistry, Princeton University

DOI: https://doi.org/10.1038/ncomms10589
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 9

Abstract

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The ubiquitylation of histone H2B on lysine 120 is an important modification with roles in a diverse range of nuclear processes. Here, the authors use 'designer' chromatin to show that H2B-ub orients hDot1L into the correct position for activation.

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/

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