ArticleJournal of virology2008
Ty3 nucleocapsid controls localization of particle assembly.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Mapping the structural landscape of the yeast Ty3 retrotransposon RNA genome.Nucleic acids research · 2024Article
- Article
- UBQLN2 restrains the domesticated retrotransposon PEG10 to maintain neuronal health in ALS.eLife · 2023Article
- Meiotic Cells Counteract Programmed Retrotransposon Activation via RNA-Binding Translational Repressor Assemblies.Developmental cell · 2021Article
- Visualizing Association of the Retroviral Gag Protein with Unspliced Viral RNA in the Nucleus.mBio · 2020Article
- Identifying the assembly intermediate in which Gag first associates with unspliced HIV-1 RNA suggests a novel model for HIV-1 RNA packaging.PLoS pathogens · 2018Article
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions.Nucleic acids research · 2015Article
- A trans-dominant form of Gag restricts Ty1 retrotransposition and mediates copy number control.Journal of virology · 2015Article
- The Influence of LINE-1 and SINE Retrotransposons on Mammalian Genomes.Microbiology spectrum · 2015Review
- Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.PLoS genetics · 2015Article
- Nuclear trafficking of retroviral RNAs and Gag proteins during late steps of replication.Viruses · 2013Review
- Sequence requirements for localization and packaging of Ty3 retroelement RNA.Virus research · 2013Article
- Ty1 gag enhances the stability and nuclear export of Ty1 mRNA.Traffic (Copenhagen, Denmark) · 2013Article
- Modulation of hepatitis C virus RNA accumulation and translation by DDX6 and miR-122 are mediated by separate mechanisms.PloS one · 2013Article
- Global identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP).The Journal of biological chemistry · 2012Article
- HIV-1 Gag co-opts a cellular complex containing DDX6, a helicase that facilitates capsid assembly.The Journal of cell biology · 2012Article
- Telomerase and retrotransposons: reverse transcriptases that shaped genomes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The TY3 Gag3 spacer controls intracellular condensation and uncoating.Journal of virology · 2011Article
- Two-hybrid analysis of Ty3 capsid subdomain interactions.Mobile DNA · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Expression of the budding yeast retrotransposon Ty3 results in production of viruslike particles (VLPs) and retrotransposition. The Ty3 major structural protein, Gag3, similar to retrovirus Gag, is processed into capsid, spacer, and nucleocapsid (NC) during VLP maturation. The 57-amino-acid Ty3 NC protein has 17 basic amino acids and contains one copy of the CX(2)CX(4)HX(4)C zinc-binding motif found in retrovirus NC proteins. Ty3 RNA, protein, and VLPs accumulate in clusters associated with RNA processing bodies (P bodies). This study investigated the role of the NC domain in Ty3-P body clustering and VLP assembly. Fifteen Ty3 NC Ala substitution and deletion mutants were examined using transposition, immunoblot, RNA protection, cDNA synthesis, and multimerization assays. Localization of Ty3 proteins and VLPs was characterized microscopically. Substitutions of each of the conserved residues of the zinc-binding motif resulted in the loss of Ty3 RNA packaging. Substitution of the first two of four conserved residues in this motif caused the loss of Ty3 RNA and protein clustering with P bodies and disrupted particle formation. NC was shown to be a mediator of formation of Ty3 RNA foci and association of Ty3 RNA and protein with P bodies. Mutations that disrupted these NC functions resulted in various degrees of Gag3 nuclear localization and a spectrum of different particle states. Our findings are consistent with the model that Ty3 assembly is associated with P-body components. We hypothesize that the NC domain acts as a molecular switch to control Gag3 conformational states that affect both assembly and localization.
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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.