5AV6

human nucleosome core particle

5AV6 の概要

• エントリーDOI: 10.2210/pdb5av6/pdb
• 関連するPDBエントリー: 5AV5 5AV8 5AV9 5AVB 5AVC
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
• 機能のキーワード: nucleosome core particle, ncp, acetylation, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: P68431 P62805 P04908 P06899
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 203168.75

構造登録者

Wakamori, M.,Fujii, Y.,Umehara, T.,Yokoyama, S. (登録日: 2015-06-12, 公開日: 2015-12-23, 最終更新日: 2024-03-20)

主引用文献

Wakamori, M.,Fujii, Y.,Suka, N.,Shirouzu, M.,Sakamoto, K.,Umehara, T.,Yokoyama, S.
Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation
Sci Rep, 5:17204-17204, 2015

PubMed Abstract: Post-translational modifications (PTMs) of histones, such as lysine acetylation of the N-terminal tails, play crucial roles in controlling gene expression. Due to the difficulty in reconstituting site-specifically acetylated nucleosomes with crystallization quality, structural analyses of histone acetylation are currently performed using synthesized tail peptides. Through engineering of the genetic code, translation termination, and cell-free protein synthesis, we reconstituted human H4-mono- to tetra-acetylated nucleosome core particles (NCPs), and solved the crystal structures of the H4-K5/K8/K12/K16-tetra-acetylated NCP and unmodified NCP at 2.4 Å and 2.2 Å resolutions, respectively. The structure of the H4-tetra-acetylated NCP resembled that of the unmodified NCP, and the DNA wrapped the histone octamer as precisely as in the unmodified NCP. However, the B-factors were significantly increased for the peripheral DNAs near the N-terminal tail of the intra- or inter-nucleosomal H4. In contrast, the B-factors were negligibly affected by the H4 tetra-acetylation in histone core residues, including those composing the acidic patch, and at H4-R23, which interacts with the acidic patch of the neighboring NCP. The present study revealed that the H4 tetra-acetylation impairs NCP self-association by changing the interactions of the H4 tail with DNA, and is the first demonstration of crystallization quality NCPs reconstituted with genuine PTMs.

PubMed: 26607036
DOI: 10.1038/srep17204

実験手法

X-RAY DIFFRACTION (2.2 Å)