5YGC

Crystal structure of Drosophila melanogaster Papi extended Tudor domain

5YGC の概要

• エントリーDOI: 10.2210/pdb5ygc/pdb
• 分子名称: GH18329p (2 entities in total)
• 機能のキーワード: pirna, papi, extended tudor domain, protein binding
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25156.57

構造登録者

Zhang, Y.H.,Huang, Y. (登録日: 2017-09-22, 公開日: 2018-03-14, 最終更新日: 2023-11-22)

主引用文献

Zhang, Y.,Liu, W.,Li, R.,Gu, J.,Wu, P.,Peng, C.,Ma, J.,Wu, L.,Yu, Y.,Huang, Y.
Structural insights into the sequence-specific recognition of Piwi byDrosophilaPapi
Proc. Natl. Acad. Sci. U.S.A., 115:3374-3379, 2018

PubMed Abstract: The Tudor domain-containing (Tdrd) family proteins play a critical role in transposon silencing in animal gonads by recognizing the symmetrically dimethylated arginine (sDMA) on the (G/A)R motif of the N-terminal of PIWI family proteins via the eTud domains. Papi, also known as "Tdrd2," is involved in Zucchini-mediated PIWI-interacting RNA (piRNA) 3'-end maturation. Intriguingly, a recent study showed that, in mutant flies, only Piwi-bound piRNAs increased in length, and not Ago3-bound or Aub-bound piRNAs. However, the molecular and structural basis of the Papi-Piwi complex is still not fully understood, which limits mechanistic understanding of the function of Papi in piRNA biogenesis. In the present study, we determined the crystal structures of Papi-eTud in the apo form and in complex with a peptide containing unmethylated or dimethylated R10 residues. Structural and biochemical analysis showed that the Papi interaction region on the Piwi contains an RGRRR motif (R7-R11) distinct from the consensus (G/A)R motif recognized by canonical eTud. Mass spectrometry results indicated that Piwi is the major binding partner of Papi in vivo. The mutant flies suffered from both fertility and transposon-silencing defects, supporting the important role conferred to Papi in piRNA 3' processing through direct interaction with Piwi proteins.

PubMed: 29531043
DOI: 10.1073/pnas.1717116115

実験手法

X-RAY DIFFRACTION (2 Å)