ArticleThe Journal of biological chemistry2016
Ty1 Integrase Interacts with RNA Polymerase III-specific Subcomplexes to Promote Insertion of Ty1 Elements Upstream of Polymerase (Pol) III-transcribed Genes.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 28 citations in OpenAlex.
- Progresses of transposon research inSynthetic and systems biotechnology · 2026Review
- Host-transposable element coexistence: a matter of resistance, tolerance and trade-off.The EMBO journal · 2026Review
- Evolutionary Consequences of Unusually Large Pericentric TE-rich Regions in the Genome of a Neotropical Fig Wasp.Genome biology and evolution · 2025Article
- Evolution of a Restriction Factor by Domestication of a Yeast Retrotransposon.Molecular biology and evolution · 2024Article
- An interchangeable prion-like domain is required for Ty1 retrotransposition.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.Nature communications · 2023Article
- A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition.Mobile DNA · 2022Article
- Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes.Nature communications · 2021Article
- Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families.Current genetics · 2021Review
- A small targeting domain in Ty1 integrase is sufficient to direct retrotransposon integration upstream of tRNA genes.The EMBO journal · 2020Article
- Transposable elements employ distinct integration strategies with respect to transcriptional landscapes in eukaryotic genomes.Nucleic acids research · 2020Article
- Evolution of Ty1 copy number control in yeast by horizontal transfer and recombination.PLoS genetics · 2020Article
- Integrating transposable elements in the 3D genome.Mobile DNA · 2020Article
- Diverse transposable element landscapes in pathogenic and nonpathogenic yeast models: the value of a comparative perspective.Mobile DNA · 2020Review
- Convergent evolution of integration site selection upstream of tRNA genes by yeast and amoeba retrotransposons.Nucleic acids research · 2018Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 2018Article
- Retrotransposon targeting to RNA polymerase III-transcribed genes.Mobile DNA · 2018Review
- Ribosome Biogenesis Modulates Ty1 Copy Number Control inGenetics · 2017Article
- Integration site selection by retroviruses and transposable elements in eukaryotes.Nature reviews. Genetics · 2017Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Retrotransposons are eukaryotic mobile genetic elements that transpose by reverse transcription of an RNA intermediate and are derived from retroviruses. The Ty1 retrotransposon of Saccharomyces cerevisiae belongs to the Ty1/Copia superfamily, which is present in every eukaryotic genome. Insertion of Ty1 elements into the S. cerevisiae genome, which occurs upstream of genes transcribed by RNA Pol III, requires the Ty1 element-encoded integrase (IN) protein. Here, we report that Ty1-IN interacts in vivo and in vitro with RNA Pol III-specific subunits to mediate insertion of Ty1 elements upstream of Pol III-transcribed genes. Purification of Ty1-IN from yeast cells followed by mass spectrometry (MS) analysis identified an enrichment of peptides corresponding to the Rpc82/34/31 and Rpc53/37 Pol III-specific subcomplexes. GFP-Trap purification of multiple GFP-tagged RNA Pol III subunits from yeast extracts revealed that the majority of Pol III subunits co-purify with Ty1-IN but not two other complexes required for Pol III transcription, transcription initiation factors (TF) IIIB and IIIC. In vitro binding studies with bacterially purified RNA Pol III proteins demonstrate that Rpc31, Rpc34, and Rpc53 interact directly with Ty1-IN. Deletion of the N-terminal 280 amino acids of Rpc53 abrogates insertion of Ty1 elements upstream of the hot spot SUF16 tRNA locus and abolishes the interaction of Ty1-IN with Rpc37. The Rpc53/37 complex therefore has an important role in targeting Ty1-IN to insert Ty1 elements upstream of Pol III-transcribed genes.
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Registered trials
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