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

Nature communications, 2019-02, Vol.10 (1), p.576-576, Article 576 [Peer Reviewed Journal]

This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2019 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-019-08314-x ;PMID: 30718488

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Title:
The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
Author: Arimura, Yasuhiro ; Tachiwana, Hiroaki ; Takagi, Hiroki ; Hori, Tetsuya ; Kimura, Hiroshi ; Fukagawa, Tatsuo ; Kurumizaka, Hitoshi
Subjects: Animals ; Blotting, Western ; Cell Line ; Centromere - genetics ; Centromere - metabolism ; Centromere Protein A - genetics ; Centromere Protein A - metabolism ; Chickens ; Crystal structure ; Glutamine ; Histone H3 ; Histone H4 ; Histones ; Humans ; Lysine ; Methylation ; Mutation ; Mutation - genetics ; Nucleosomes ; Nucleosomes - genetics ; Nucleosomes - metabolism ; Polymorphism ; Polymorphism, Genetic - genetics ; Relocation ; Valine
Is Part Of: Nature communications, 2019-02, Vol.10 (1), p.576-576, Article 576
Description: Centromeric nucleosomes are composed of the centromere-specific histone H3 variant CENP-A and the core histones H2A, H2B, and H4. To establish a functional kinetochore, histone H4 lysine-20 (H4K20) must be monomethylated, but the underlying mechanism has remained enigmatic. To provide structural insights into H4K20 methylation, we here solve the crystal structure of a nucleosome containing an H3.1-CENP-A chimera, H3.1 , which has a CENP-A centromere targeting domain and preserves essential CENP-A functions in vivo. Compared to the canonical H3.1 nucleosome, the H3.1 nucleosome exhibits conformational changes in the H4 N-terminal tail leading to a relocation of H4K20. In particular, the H4 N-terminal tail interacts with glutamine-76 and aspartate-77 of canonical H3.1 while these interactions are cancelled in the presence of the CENP-A-specific residues valine-76 and lysine-77. Mutations of valine-76 and lysine-77 impair H4K20 monomethylation both in vitro and in vivo. These findings suggest that a CENP-A-mediated structural polymorphism may explain the preferential H4K20 monomethylation in centromeric nucleosomes.
Publisher: England: Nature Publishing Group
Language: English
Identifier: ISSN: 2041-1723
EISSN: 2041-1723
DOI: 10.1038/s41467-019-08314-x
PMID: 30718488
Source: MEDLINE
PubMed Central
ProQuest Central
DOAJ Directory of Open Access Journals

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

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