ArticleNature communications2023
Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 8 citations in OpenAlex.
- Progresses of transposon research inSynthetic and systems biotechnology · 2026Review
- Alpha-like subunits of multisubunit RNA polymerases: insights into structure, function, and disease.RNA biology · 2026Review
- Optimized cryo-FIB milling strategy to generate thin, minimally damaged biological lamellae.bioRxiv : the preprint server for biology · 2026Article
- GeoPep: A Geometry-Aware Masked Language Model for Protein-Peptide Binding Site Prediction.Journal of chemical information and modeling · 2026Article
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- Whitefly transmitted begomovirus infection in plant and host response: a review.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- Cryo-EM uncovers a sequential mechanism for RNA polymerase I pausing and stalling at abasic DNA lesions.Nature communications · 2025Article
- From parasites to partners: exploring the intricacies of host-transposon dynamics and coevolution.Functional & integrative genomics · 2023Review
- Reproducible evaluation of transposable element detectors with McClintock 2 guides accurate inference of Ty insertion patterns in yeast.Mobile DNA · 2023Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and Pol III, currently uncharacterized at the atomic level. We report cryo-EM structures of Pol III in complex with IN1, revealing a 16-residue segment at the IN1 C-terminus that contacts Pol III subunits AC40 and AC19, an interaction that we validate by in vivo mutational analysis. Binding to IN1 associates with allosteric changes in Pol III that may affect its transcriptional activity. The C-terminal domain of subunit C11, involved in RNA cleavage, inserts into the Pol III funnel pore, providing evidence for a two-metal mechanism during RNA cleavage. Additionally, ordering next to C11 of an N-terminal portion from subunit C53 may explain the connection between these subunits during termination and reinitiation. Deletion of the C53 N-terminal region leads to reduced chromatin association of Pol III and IN1, and a major fall in Ty1 integration events. Our data support a model in which IN1 binding induces a Pol III configuration that may favor its retention on chromatin, thereby improving the likelihood of Ty1 integration.
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Registered trials
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.