ArticleNature communications2021
Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes.
Article in Nature communications, 2021. 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, 17 citations in OpenAlex.
- The Portuguese man-of-war genome reveals the genetic basis of medusa loss and sea-air interface adaptation.National science review · 2026Article
- A functional atlas of transposon-encoded products and their integration into host networks.Nature communications · 2026Article
- Transcriptional profiles of the fish parasite Neoechinorhynchus agilis (Acanthocephala) emphasize energetic stress in males and high cell-division activity in females.BMC genomics · 2025Article
- Evolution of Einkorn wheat centromeres is driven by the mutualistic interplay of two LTR retrotransposons.Mobile DNA · 2024Article
- The structure, function, and evolution of plant centromeres.Genome research · 2024Review
- The Dynamic Interplay Between Ribosomal DNA and Transposable Elements: A Perspective From Genomics and Cytogenetics.Molecular biology and evolution · 2024Article
- Article
- Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.Nature communications · 2023Article
- Multivalent interactions essential for lentiviral integrase function.Nature communications · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Retrotransposons are endogenous elements that have the ability to mobilise their DNA between different locations in the host genome. The Ty3 retrotransposon integrates with an exquisite specificity in a narrow window upstream of RNA Polymerase (Pol) III-transcribed genes, representing a paradigm for harmless targeted integration. Here we present the cryo-EM reconstruction at 4.0 Å of an active Ty3 strand transfer complex bound to TFIIIB transcription factor and a tRNA gene. The structure unravels the molecular mechanisms underlying Ty3 targeting specificity at Pol III-transcribed genes and sheds light into the architecture of retrotransposon machinery during integration. Ty3 intasome contacts a region of TBP, a subunit of TFIIIB, which is blocked by NC2 transcription regulator in RNA Pol II-transcribed genes. A newly-identified chromodomain on Ty3 integrase interacts with TFIIIB and the tRNA gene, defining with extreme precision the integration site position.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.