ArticleMolecular and cellular biology2010
P-body components are required for Ty1 retrotransposition during assembly of retrotransposition-competent virus-like particles.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed, 77 citations in OpenAlex.
- GAG Protein ofPlants (Basel, Switzerland) · 2025Article
- LINE-1 mRNA 3' end dynamics shape its biology and retrotransposition potential.Nucleic acids research · 2024Article
- Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 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
- Ribonucleoprotein Granules: Between Stress and Transposable Elements.Biomolecules · 2023Review
- An interchangeable prion-like domain is required for Ty1 retrotransposition.bioRxiv : the preprint server for biology · 2023Article
- Reliance of Host-Encoded Regulators of Retromobility on Ty1 Promoter Activity or Architecture.Frontiers in molecular biosciences · 2022Article
- Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.Nature communications · 2021Article
- RNA Binding Properties of the Ty1 LTR-Retrotransposon Gag Protein.International journal of molecular sciences · 2021Article
- Diverse transposable element landscapes in pathogenic and nonpathogenic yeast models: the value of a comparative perspective.Mobile DNA · 2020Review
- Viral Regulation of RNA Granules in Infected Cells.Virologica Sinica · 2019Review
- Control of yeast retrotransposons mediated through nucleoporin evolution.PLoS genetics · 2018Article
- Article
- The Mediator co-activator complex regulates Ty1 retromobility by controlling the balance between Ty1i and Ty1 promoters.PLoS genetics · 2018Article
- Ribosome Biogenesis Modulates Ty1 Copy Number Control inGenetics · 2017Article
- Paralog-Specific Functions ofG3 (Bethesda, Md.) · 2017Article
- The histone methyltransferases Set5 and Set1 have overlapping functions in gene silencing and telomere maintenance.Epigenetics · 2017Article
- XRN1 Is a Species-Specific Virus Restriction Factor in Yeasts.PLoS pathogens · 2016Article
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces.Current genetics · 2016Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Ty1 is a retrovirus-like retrotransposon whose replication is influenced by diverse cellular processes in Saccharomyces cerevisiae. We have identified cytoplasmic P-body components encoded by DHH1, KEM1, LSM1, and PAT1 as cofactors that posttranscriptionally enhance Ty1 retrotransposition. Using fluorescent in situ hybridization and immunofluorescence microscopy, we found that Ty1 mRNA and Gag colocalize to discrete cytoplasmic foci in wild-type cells. These foci, which are distinct from P-bodies, do not form in P-body component mutants or under conditions suboptimal for retrotransposition. Our immunoelectron microscopy (IEM) data suggest that mRNA/Gag foci are sites where virus-like particles (VLPs) cluster. Overexpression of Ty1 leads to a large increase in retrotransposition in wild-type cells, which allows VLPs to be detected by IEM. However, retrotransposition is still reduced in P-body component mutants under these conditions. Moreover, the percentage of Ty1 mRNA/Gag foci and VLP clusters and levels of integrase and reverse transcriptase are reduced in these mutants. Ty1 antisense RNAs, which have been reported to inhibit Ty1 transposition, are more abundant in the kem1Delta mutant and colocalize with Ty1 mRNA in the cytoplasm. Therefore, Kem1p may prevent the aggregation of Ty1 antisense and mRNAs. Overall, our results suggest that P-body components enhance the formation of retrotransposition-competent Ty1 VLPs.
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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.