Structural and biochemical analyses of monoubiquitinated human histones H2B and H4

Shinichi Machida, Satoshi Sekine, Yuuki Nishiyama, Naoki Horikoshi, Hitoshi Kurumizaka

研究成果: Article

18 引用 (Scopus)

抄録

Monoubiquitination is a major histone post-translational modification. In humans, the histone H2B K120 and histone H4 K31 residues are monoubiquitinated and may form transcriptionally active chromatin. In this study, we reconstituted nucleosomes containing H2B monoubiquitinated at position 120 (H2Bub120 ) and/or H4 monoubiquitinated at position 31 (H4ub31 ). We found that the H2Bub120 and H4ub31 monoubiquitinations differently affect nucleosome stability: the H2Bub120 monoubiquitination enhances the H2A- H2B association with the nucleosome, while the H4ub31 monoubiquitination decreases the H3-H4 stability in the nucleosome, when compared with the unmodified nucleosome. The H2Bub120 and H4ub31 monoubiquitinations both antagonize the Mg2+ -dependent compaction of a poly-nucleosome, suggesting that these monoubiquitinations maintain more relaxed conformations of chromatin. In the crystal structure, the H2Bub120 and H4ub31 monoubiquitinations do not change the structure of the nucleosome core particle and the ubiquitin molecules were flexibly disordered in the H2Bub120 /H4ub31 nucleosome structure. These results revealed the differences and similarities of the H2Bub120 and H4ub31 monoubiquitinations at the mono- and poly-nucleosome levels and provide novel information to clarify the roles of monoubiquitination in chromatin.

元の言語English
記事番号160090
ジャーナルOpen Biology
6
発行部数6
DOI
出版物ステータスPublished - 2016 6 1

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Nucleosomes
Histones
Chromatin
Post Translational Protein Processing
Ubiquitin
Conformations
Compaction
Crystal structure
Association reactions
Molecules

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Neuroscience(all)
  • Immunology

これを引用

Machida, S., Sekine, S., Nishiyama, Y., Horikoshi, N., & Kurumizaka, H. (2016). Structural and biochemical analyses of monoubiquitinated human histones H2B and H4. Open Biology, 6(6), [160090]. https://doi.org/10.1098/rsob.160090

Structural and biochemical analyses of monoubiquitinated human histones H2B and H4. / Machida, Shinichi; Sekine, Satoshi; Nishiyama, Yuuki; Horikoshi, Naoki; Kurumizaka, Hitoshi.

:: Open Biology, 巻 6, 番号 6, 160090, 01.06.2016.

研究成果: Article

Machida, S, Sekine, S, Nishiyama, Y, Horikoshi, N & Kurumizaka, H 2016, 'Structural and biochemical analyses of monoubiquitinated human histones H2B and H4', Open Biology, 巻. 6, 番号 6, 160090. https://doi.org/10.1098/rsob.160090
Machida S, Sekine S, Nishiyama Y, Horikoshi N, Kurumizaka H. Structural and biochemical analyses of monoubiquitinated human histones H2B and H4. Open Biology. 2016 6 1;6(6). 160090. https://doi.org/10.1098/rsob.160090
Machida, Shinichi ; Sekine, Satoshi ; Nishiyama, Yuuki ; Horikoshi, Naoki ; Kurumizaka, Hitoshi. / Structural and biochemical analyses of monoubiquitinated human histones H2B and H4. :: Open Biology. 2016 ; 巻 6, 番号 6.
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