7VRF

Crystal structure of Oxpecker chromodomain in complex with H3K9me3

7VRF の概要

• エントリーDOI: 10.2210/pdb7vrf/pdb
• 分子名称: Oxpecker, H3K9me3 (3 entities in total)
• 機能のキーワード: chromodomain, histone binding, gene regulation
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 19536.25

構造登録者

Huang, Y.,Jin, Z.,Yu, B. (登録日: 2021-10-22, 公開日: 2022-10-26, 最終更新日: 2023-11-29)

主引用文献

Jin, Z.,Yu, B.,Huang, Y.
Structural insights into the chromodomain of Oxpecker in complex with histone H3 lysine 9 trimethylation reveal a transposon silencing mechanism by heterodimerization.
Biochem.Biophys.Res.Commun., 652:95-102, 2023

PubMed Abstract: Oxpecker, the homolog of Rhino/HP1D, exclusively expressed in Drosophila ovaries, belongs to the Heterochromatin Protein 1 family, as does Rhino. Rhi recognizes piRNA clusters enriched with the heterochromatin marker H3K9me3 via its N-terminal chromodomain and recruits Deadlock via its C-terminal chromoshadow domain, further recruits Moonshiner, a paralog of the TATA box-binding protein-related factor 2 large subunits, to promote transcription of piRNA precursors, thereby protecting the genome. Despite Oxp possessing only the chromodomain, its loss leads to the upregulation of transposons in the female germline. In this study, we solved the crystal structure of the Oxp chromodomain in complex with the histone H3K9me3 peptide. As the Oxp chromodomain dimerizes, two H3K9me3 peptides bind to the Oxp chromodomain in an antiparallel manner. ITC experiments and site-directed mutagenesis experiments showed that E44 determines Oxp's five-fold stronger binding ability to H3K9me3 than that of Rhi. In addition, we found that Oxp and Rhi can form a heterodimer, which may shed light on the molecular mechanism by which Oxp regulates transposon silencing in the absence of CSD.

PubMed: 36841100
DOI: 10.1016/j.bbrc.2023.02.045

実験手法

X-RAY DIFFRACTION (1.7 Å)