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

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 t...

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Main Authors: Yasuhiro Arimura, Hiroaki Tachiwana, Hiroki Takagi, Tetsuya Hori, Hiroshi Kimura, Tatsuo Fukagawa, Hitoshi Kurumizaka
Format: Article
Language:English
Published: Nature Portfolio 2019-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-08314-x
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author Yasuhiro Arimura
Hiroaki Tachiwana
Hiroki Takagi
Tetsuya Hori
Hiroshi Kimura
Tatsuo Fukagawa
Hitoshi Kurumizaka
author_facet Yasuhiro Arimura
Hiroaki Tachiwana
Hiroki Takagi
Tetsuya Hori
Hiroshi Kimura
Tatsuo Fukagawa
Hitoshi Kurumizaka
author_sort Yasuhiro Arimura
collection DOAJ
description 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.
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spelling doaj.art-b792e5547ea1411d9cc207781efaa5ba2022-12-21T21:21:43ZengNature PortfolioNature Communications2041-17232019-02-0110111010.1038/s41467-019-08314-xThe CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphismYasuhiro Arimura0Hiroaki Tachiwana1Hiroki Takagi2Tetsuya Hori3Hiroshi Kimura4Tatsuo Fukagawa5Hitoshi Kurumizaka6Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of TokyoGraduate School of Advanced Science and Engineering, Waseda UniversityLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of TokyoGraduate School of Frontier Biosciences, Osaka UniversityCell Biology Center, Institute of Innovative Research, Tokyo Institute of TechnologyGraduate School of Frontier Biosciences, Osaka UniversityLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of TokyoKinetochore 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.https://doi.org/10.1038/s41467-019-08314-x
spellingShingle Yasuhiro Arimura
Hiroaki Tachiwana
Hiroki Takagi
Tetsuya Hori
Hiroshi Kimura
Tatsuo Fukagawa
Hitoshi Kurumizaka
The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
Nature Communications
title The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
title_full The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
title_fullStr The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
title_full_unstemmed The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
title_short The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
title_sort cenp a centromere targeting domain facilitates h4k20 monomethylation in the nucleosome by structural polymorphism
url https://doi.org/10.1038/s41467-019-08314-x
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