ArticleNucleic acids research2008
The Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus.
Article in Nucleic acids research, 2008. 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, 40 citations in OpenAlex.
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition.Mobile DNA · 2022Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- Genome-wide characterization of LTR retrotransposons in the non-model deep-sea annelid Lamellibrachia luymesi.BMC genomics · 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
- Diverse transposable element landscapes in pathogenic and nonpathogenic yeast models: the value of a comparative perspective.Mobile DNA · 2020Review
- Additional ORFs in Plant LTR-Retrotransposons.Frontiers in plant science · 2020Review
- Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.Biochemistry · 2019Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 2018Article
- Control of yeast retrotransposons mediated through nucleoporin evolution.PLoS genetics · 2018Article
- Ribosome Biogenesis Modulates Ty1 Copy Number Control inGenetics · 2017Article
- Integration site selection by retroviruses and transposable elements in eukaryotes.Nature reviews. Genetics · 2017Review
- Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins.The Journal of biological chemistry · 2016Article
- A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces.Current genetics · 2016Review
- The Ty1 LTR-retrotransposon of budding yeast,Microbiology spectrum · 2015Article
- A role for the budding yeast separase, Esp1, in Ty1 element retrotransposition.PLoS genetics · 2015Article
- A subset of FG-nucleoporins is necessary for efficient Msn5-mediated nuclear protein export.Biochimica et biophysica acta · 2013Article
- Grande retrotransposons contain an accessory gene in the unusually long 3'-internal region that encodes a nuclear protein transcribed from its own promoter.Plant molecular biology · 2013Article
- Highly diverse chromoviruses of Beta vulgaris are classified by chromodomains and chromosomal integration.Mobile DNA · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Like its retroviral relatives, the long terminal repeat retrotransposon Ty1 in the yeast Saccharomyces cerevisiae must traverse a permanently intact nuclear membrane for successful transposition and replication. For retrotransposition to occur, at least a subset of Ty1 proteins, including the Ty1 integrase, must enter the nucleus. Nuclear localization of integrase is dependent upon a C-terminal nuclear targeting sequence. However, the nuclear import machinery that recognizes this nuclear targeting signal has not been defined. We investigated the mechanism by which Ty1 integrase gains access to nuclear DNA as a model for how other retroelements, including retroviruses like HIV, may utilize cellular nuclear transport machinery to import their essential nuclear proteins. We show that Ty1 retrotransposition is significantly impaired in yeast mutants that alter the classical nuclear protein import pathway, including the Ran-GTPase, and the dimeric import receptor, importin-alpha/beta. Although Ty1 proteins are made and processed in these mutant cells, our studies reveal that an integrase reporter is not properly targeted to the nucleus in cells carrying mutations in the classical nuclear import machinery. Furthermore, we demonstrate that integrase coimmunoprecipitates with the importin-alpha transport receptor and directly binds to importin-alpha. Taken together, these data suggest Ty1 integrase can employ the classical nuclear protein transport machinery to enter the nucleus.
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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.