ArticleScience advances2025
Structures of vertebrate R2 retrotransposon complexes during target-primed reverse transcription and after second-strand nicking.
Article in Science advances, 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.
- Programmable enzymes for targeted gene insertion.Nature reviews. Genetics · 2026Review
- DNA-bound avian R2 non-LTR retrotransposon protein recruits a second R2 protein for genome-protective second-strand nicking.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Efficient site-specific gene addition using R2 retrotransposons in tobacco and rice.Nature biotechnology · 2026Article
- Optimized R2 retroelement complexes for DNA insertion into plant genomes.Nature biotechnology · 2026Article
- Lineage-specific evolution, structural diversity, and activity of R2 retrotransposons in animals.Genome biology · 2026Article
- Single-turnover kinetic analysis of non-long terminal repeat retrotransposition defines the pathway and rate constants leading to second-strand synthesis.Nucleic acids research · 2026Article
- Rewriting the genome: harnessing R2 retrotransposons for precise DNA insertion.Frontiers in genome editing · 2026Review
- Biology and utilization of R2 retrotransposons.RNA biology · 2025Review
- Structural and biochemical studies of mobile retrotransposon proteins in action.Current opinion in structural biology · 2025Review
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Abstract
R2 retrotransposons are site-specific eukaryotic non-long terminal repeat retrotransposons that copy and paste into gene loci encoding ribosomal RNAs. Recently, we demonstrated that avian A-clade R2 proteins achieve efficient and precise insertion of transgenes into their native safe-harbor loci in human cells. The features of A-clade R2 proteins that support gene insertion are not well characterized. Here, we report high-resolution cryo-electron microscopy structures of two vertebrate A-clade R2 proteins at the initiation of target-primed reverse transcription and after cDNA synthesis and second-strand nicking. Using biochemical and cellular assays, we illuminate the basis for high selectivity of template use and unique roles for each of the three zinc-finger domains in nucleic acid recognition. Reverse transcriptase active site architecture is reinforced by an unanticipated insertion motif specific to vertebrate A-clade R2 proteins. Our work provides the first insights into A-clade R2 protein structure during gene insertion and may enable future improvement and adaptation of R2-based systems for precise transgene insertion.
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