7CFD

Drosophila melanogaster Krimper eTud2-AubR15me2 complex

7CFD の概要

• エントリーDOI: 10.2210/pdb7cfd/pdb
• 分子名称: FI20010p1, Protein aubergine (3 entities in total)
• 機能のキーワード: pirna ampilication, gene silencing, 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: 16
• 化学式量合計: 184756.42

構造登録者

Hu, H.,Li, S. (登録日: 2020-06-25, 公開日: 2021-06-02, 最終更新日: 2024-11-13)

主引用文献

Huang, X.,Hu, H.,Webster, A.,Zou, F.,Du, J.,Patel, D.J.,Sachidanandam, R.,Toth, K.F.,Aravin, A.A.,Li, S.
Binding of guide piRNA triggers methylation of the unstructured N-terminal region of Aub leading to assembly of the piRNA amplification complex.
Nat Commun, 12:4061-4061, 2021

PubMed Abstract: PIWI proteins use guide piRNAs to repress selfish genomic elements, protecting the genomic integrity of gametes and ensuring the fertility of animal species. Efficient transposon repression depends on amplification of piRNA guides in the ping-pong cycle, which in Drosophila entails tight cooperation between two PIWI proteins, Aub and Ago3. Here we show that post-translational modification, symmetric dimethylarginine (sDMA), of Aub is essential for piRNA biogenesis, transposon silencing and fertility. Methylation is triggered by loading of a piRNA guide into Aub, which exposes its unstructured N-terminal region to the PRMT5 methylosome complex. Thus, sDMA modification is a signal that Aub is loaded with piRNA guide. Amplification of piRNA in the ping-pong cycle requires assembly of a tertiary complex scaffolded by Krimper, which simultaneously binds the N-terminal regions of Aub and Ago3. To promote generation of new piRNA, Krimper uses its two Tudor domains to bind Aub and Ago3 in opposite modification and piRNA-loading states. Our results reveal that post-translational modifications in unstructured regions of PIWI proteins and their binding by Tudor domains that are capable of discriminating between modification states is essential for piRNA biogenesis and silencing.

PubMed: 34210982
DOI: 10.1038/s41467-021-24351-x

実験手法

X-RAY DIFFRACTION (2.704 Å)