3F8J

Mouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group C222(1)

3F8J の概要

• エントリーDOI: 10.2210/pdb3f8j/pdb
• 関連するPDBエントリー: 2ZO0 2ZO1 2ZO2 3F8I
• 分子名称: E3 ubiquitin-protein ligase UHRF1, 5'-D(*DCP*DCP*DAP*DTP*DGP*(5CM)P*DGP*DCP*DTP*DGP*DAP*DC)-3', 5'-D(*DGP*DTP*DCP*DAP*DGP*DCP*DGP*DCP*DAP*DTP*DGP*DG)-3', ... (5 entities in total)
• 機能のキーワード: uhrf1, sra, base flipping, 5-methylcytosine, cpg methylation, cell cycle, developmental protein, dna damage, dna repair, dna-binding, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation pathway, zinc-finger, ligase-dna complex, ligase/dna
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Nucleus: Q8VDF2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32028.31

構造登録者

Hashimoto, H.,Horton, J.R.,Zhang, X.,Cheng, X. (登録日: 2008-11-12, 公開日: 2009-01-06, 最終更新日: 2023-09-06)

主引用文献

Hashimoto, H.,Horton, J.R.,Zhang, X.,Cheng, X.
UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications.
Epigenetics, 4:8-14, 2009

PubMed Abstract: Cytosine methylation in DNA is a major epigenetic signal, and plays a central role in propagating chromatin status during cell division. However the mechanistic links between DNA methylation and histone methylation are poorly understood. A multi-domain protein UHRF1 (ubiquitin-like, containing PHD and RING finger domains 1) is required for DNA CpG maintenance methylation at replication forks, and mouse UHRF1-null cells show enhanced susceptibility to DNA replication arrest and DNA damaging agents. Recent data demonstrated that the SET and RING associated (SRA) domain of UHRF1 binds hemimethylated CpG and flips 5-methylcytosine out of the DNA helix, whereas its tandom tudor domain and PHD domain bind the tail of histone H3 in a highly methylation sensitive manner. We hypothesize that UHRF1 brings the two components (histones and DNA) carrying appropriate markers (on the tails of H3 and hemimethylated CpG sites) ready to be assembled into a nucleosome after replication.

PubMed: 19077538

実験手法

X-RAY DIFFRACTION (1.99 Å)