5IAY

NMR structure of UHRF1 Tandem Tudor Domains in a complex with Spacer peptide

5IAY の概要

• エントリーDOI: 10.2210/pdb5iay/pdb
• NMR情報: BMRB: 30019
• 分子名称: E3 ubiquitin-protein ligase UHRF1, Spacer (2 entities in total)
• 機能のキーワード: uhrf1, ttd, spacer, ligase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q96T88
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19411.72

構造登録者

Fang, J.,Cheng, J.,Wang, J.,Zhang, Q.,Liu, M.,Gong, R.,Wang, P.,Zhang, X.,Feng, Y.,Lan, W.,Gong, Z.,Tang, C.,Wong, J.,Yang, H.,Cao, C.,Xu, Y. (登録日: 2016-02-22, 公開日: 2016-04-20, 最終更新日: 2024-05-01)

主引用文献

Fang, J.,Cheng, J.,Wang, J.,Zhang, Q.,Liu, M.,Gong, R.,Wang, P.,Zhang, X.,Feng, Y.,Lan, W.,Gong, Z.,Tang, C.,Wong, J.,Yang, H.,Cao, C.,Xu, Y.
Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition
Nat Commun, 7:11197-11197, 2016

PubMed Abstract: UHRF1 is an important epigenetic regulator for maintenance DNA methylation. UHRF1 recognizes hemi-methylated DNA (hm-DNA) and trimethylation of histone H3K9 (H3K9me3), but the regulatory mechanism remains unknown. Here we show that UHRF1 adopts a closed conformation, in which a C-terminal region (Spacer) binds to the tandem Tudor domain (TTD) and inhibits H3K9me3 recognition, whereas the SET-and-RING-associated (SRA) domain binds to the plant homeodomain (PHD) and inhibits H3R2 recognition. Hm-DNA impairs the intramolecular interactions and promotes H3K9me3 recognition by TTD-PHD. The Spacer also facilitates UHRF1-DNMT1 interaction and enhances hm-DNA-binding affinity of the SRA. When TTD-PHD binds to H3K9me3, SRA-Spacer may exist in a dynamic equilibrium: either recognizes hm-DNA or recruits DNMT1 to chromatin. Our study reveals the mechanism for regulation of H3K9me3 and hm-DNA recognition by URHF1.

PubMed: 27045799
DOI: 10.1038/ncomms11197

実験手法

SOLUTION NMR