ArticleNucleic acids research2015
Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- A retroelement-derived mammalian ARC protein exhibits selective RNA recognition and nucleic acid chaperone functions.Nucleic acids research · 2026Article
- Capsid flexibility during Ty1 virus-like particle assembly.bioRxiv : the preprint server for biology · 2025Article
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- Evolution of a Restriction Factor by Domestication of a Yeast Retrotransposon.Molecular biology and evolution · 2024Article
- Article
- Co-option of a non-retroviral endogenous viral element in planthoppers.Nature communications · 2023Article
- 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
- An interchangeable prion-like domain is required for Ty1 retrotransposition.bioRxiv : the preprint server for biology · 2023Article
- Cell Compartment-Specific Folding of Ty1 Long Terminal Repeat Retrotransposon RNA Genome.Viruses · 2022Article
- 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
- Hijacking Transposable Elements for Saturation Mutagenesis in Fungi.Frontiers in fungal biology · 2021Review
- Evolution of Ty1 copy number control in yeast by horizontal transfer and recombination.PLoS genetics · 2020Article
- Article
- Retroviral-like determinants and functions required for dimerization of Ty1 retrotransposon RNA.RNA biology · 2019Article
- Control of yeast retrotransposons mediated through nucleoporin evolution.PLoS genetics · 2018Article
- 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
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Ty1 Gag comprises the capsid of virus-like particles and provides nucleic acid chaperone (NAC) functions during retrotransposition in budding yeast. A subgenomic Ty1 mRNA encodes a truncated Gag protein (p22) that is cleaved by Ty1 protease to form p18. p22/p18 strongly inhibits transposition and can be considered an element-encoded restriction factor. Here, we show that only p22 and its short derivatives restrict Ty1 mobility whereas other regions of GAG inhibit mobility weakly if at all. Mutational analyses suggest that p22/p18 is synthesized from either of two closely spaced AUG codons. Interestingly, AUG1p18 and AUG2p18 proteins display different properties, even though both contain a region crucial for RNA binding and NAC activity. AUG1p18 shows highly reduced NAC activity but specific binding to Ty1 RNA, whereas AUG2p18 shows the converse behavior. p22/p18 affects RNA encapsidation and a mutant derivative defective for RNA binding inhibits the RNA chaperone activity of the C-terminal region (CTR) of Gag-p45. Moreover, affinity pulldowns show that p18 and the CTR interact. These results support the idea that one aspect of Ty1 restriction involves inhibition of Gag-p45 NAC functions by p22/p18-Gag interactions.
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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.