The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism

Yasuhiro Arimura; Hiroaki Tachiwana; Hiroki Takagi; Tetsuya Hori; Hiroshi Kimura; Tatsuo Fukagawa; Hitoshi Kurumizaka

doi:10.1038/s41467-019-08314-x

Nature Communications (Feb 2019)

The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism

Yasuhiro Arimura,
Hiroaki Tachiwana,
Hiroki Takagi,
Tetsuya Hori,
Hiroshi Kimura,
Tatsuo Fukagawa,
Hitoshi Kurumizaka

Affiliations

Yasuhiro Arimura: Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo
Hiroaki Tachiwana: Graduate School of Advanced Science and Engineering, Waseda University
Hiroki Takagi: Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo
Tetsuya Hori: Graduate School of Frontier Biosciences, Osaka University
Hiroshi Kimura: Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology
Tatsuo Fukagawa: Graduate School of Frontier Biosciences, Osaka University
Hitoshi Kurumizaka: Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo

DOI: https://doi.org/10.1038/s41467-019-08314-x
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

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Kinetochore function depends on H4K20 monomethylation in centromeric nucleosomes but the underlying mechanism is unclear. Here, the authors provide evidence that the centromere-specific nucleosome subunit CENP-A facilitates H4K20 methylation by enabling a conformational change of the H4 N-terminal tail.

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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