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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Format: | Article |
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Nature Portfolio
2019-02-01
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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. |
first_indexed | 2024-12-18T03:59:44Z |
format | Article |
id | doaj.art-b792e5547ea1411d9cc207781efaa5ba |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-18T03:59:44Z |
publishDate | 2019-02-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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