8S41

The structure of the copia retrotransposon icosahedral capsid (T=9)

8S41 の概要

• エントリーDOI: 10.2210/pdb8s41/pdb
• EMDBエントリー: 19643 19644 19645 19646 19647 19648 19649 19650 19651 19708
• 分子名称: Copia VLP protein (1 entity in total)
• 機能のキーワード: tomography, drosophila, melanogaster, follicle cell, copia, ty1, retrotransposon, ltr, virus like particle
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 192606.88

構造登録者

Klumpe, S.,Beck, F.,Briggs, J.A.G.,Beck, M.,Plitzko, J.M. (登録日: 2024-02-20, 公開日: 2025-03-05, 最終更新日: 2025-04-30)

主引用文献

Klumpe, S.,Senti, K.A.,Beck, F.,Sachweh, J.,Hampoelz, B.,Ronchi, P.,Oorschot, V.,Brandstetter, M.,Yeroslaviz, A.,Briggs, J.A.G.,Brennecke, J.,Beck, M.,Plitzko, J.M.
In-cell structure and snapshots of copia retrotransposons in intact tissue by cryo-ET.
Cell, 188:2094-, 2025

PubMed Abstract: Long terminal repeat (LTR) retrotransposons belong to the transposable elements (TEs), autonomously replicating genetic elements that integrate into the host's genome. Among animals, Drosophila melanogaster serves as an important model organism for TE research and contains several LTR retrotransposons, including the Ty1-copia family, which is evolutionarily related to retroviruses and forms virus-like particles (VLPs). In this study, we use cryo-focused ion beam (FIB) milling and lift-out approaches to visualize copia VLPs in ovarian cells and intact egg chambers, resolving the in situ copia capsid structure to 7.7 Å resolution by cryoelectron tomography (cryo-ET). Although cytoplasmic copia VLPs vary in size, nuclear VLPs are homogeneous and form densely packed clusters, supporting a model in which nuclear import acts as a size selector. Analyzing flies deficient in the TE-suppressing PIWI-interacting RNA (piRNA) pathway, we observe copia's translocation into the nucleus during spermatogenesis. Our findings provide insights into the replication cycle and cellular structural biology of an active LTR retrotransposon.

PubMed: 40049165
DOI: 10.1016/j.cell.2025.02.003

実験手法

ELECTRON MICROSCOPY (7.7 Å)