ArticleMolecular cell2025
A conserved PIWI silencing complex detects piRNA-target engagement.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A Novel piRNA-Mediated Epigenetic Axis: piR-36241 Exacerbates Pulpitis by Silencing the Protective Receptor ADGRG2 in Human Dental Pulp Stem Cells.International endodontic journal · 2026Article
- An evolutionarily conserved N-terminal domain of RRF-3 governs GTSF-1 binding in nematodes.EMBO reports · 2026Article
- Review
- Article
- Gametocyte-Specific Factor 1 Is Essential for Male Fertility and Transposon Homeostasis inInsects · 2026Article
- Host-transposable element coexistence: a matter of resistance, tolerance and trade-off.The EMBO journal · 2026Review
- A reference genome for cultured Drosophila ovarian somatic cells enables studies of transposon and piRNA biology.Genome biology · 2026Article
- Positive Selection Targeted Primate Genes that Encode Transposable Element Repressors.Genome biology and evolution · 2026Article
- PAIRNet: Predicting PIWI cleavage specificity via position-aware RNA interaction modeling.PLoS computational biology · 2026Article
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Authors and funding
6 authors.
Funding
Abstract
In animal germ cells, PIWI proteins use piRNAs to detect active selfish genetic elements. Base-pairing to a piRNA defines transposon recognition, but how this interaction triggers a defensive response remains unclear. Here, we identify a transposon recognition complex composed of the silkworm proteins Siwi, GTSF1, and Maelstrom. Biochemical and cryo-electron microscopy (cryo-EM) analyses show that extended piRNA-target pairing locks Siwi in a conformation that recruits GTSF1 and Maelstrom. Extended piRNA-target pairing is recognized by the N-terminal helix of Maelstrom and the first zinc finger of GTSF1, which act together to hold Siwi in an endonucleolytically active state. The resulting activated complex, termed Siwi
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Registered trials
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