ArticleJournal of virology2003
A long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe expresses a Gag-like protein that assembles into virus-like particles which mediate reverse transcription.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Identification of an integrase-independent pathway of retrotransposition.Science advances · 2022Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 2018Article
- Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.PLoS genetics · 2017Article
- Yeast for virus research.Microbial cell (Graz, Austria) · 2017Review
- Single-Nucleotide-Specific Targeting of the Tf1 Retrotransposon Promoted by the DNA-Binding Protein Sap1 of Schizosaccharomyces pombe.Genetics · 2015Article
- The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.PLoS genetics · 2015Article
- The Long Terminal Repeat Retrotransposons Tf1 and Tf2 of Schizosaccharomyces pombe.Microbiology spectrum · 2015Review
- The TY3 Gag3 spacer controls intracellular condensation and uncoating.Journal of virology · 2011Article
- Ty3 nucleocapsid controls localization of particle assembly.Journal of virology · 2008Article
- Multiple conserved domains of the nucleoporin Nup124p and its orthologs Nup1p and Nup153 are critical for nuclear import and activity of the fission yeast Tf1 retrotransposon.Molecular biology of the cell · 2007Article
- LINE-1 ORF1 protein localizes in stress granules with other RNA-binding proteins, including components of RNA interference RNA-induced silencing complex.Molecular and cellular biology · 2007Article
- Ty3 capsid mutations reveal early and late functions of the amino-terminal domain.Journal of virology · 2007Article
- Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses.Nature reviews. Microbiology · 2006Review
- Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components.RNA (New York, N.Y.) · 2006Article
- The long terminal repeat-containing retrotransposon Tf1 possesses amino acids in gag that regulate nuclear localization and particle formation.Journal of virology · 2005Article
- The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.Molecular biology of the cell · 2005Article
- Retrotransposons and their recognition of pol II promoters: a comprehensive survey of the transposable elements from the complete genome sequence of Schizosaccharomyces pombe.Genome research · 2003Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Tf1 element of Schizosaccharomyces pombe is a long terminal repeat-containing retrotransposon that encodes functional protease, reverse transcriptase, and integrase proteins. Although these proteins are known to be necessary for protein processing, reverse transcription, and integration, respectively, the function of the protein thought to be Gag has not been determined. We present here the first electron microscopy of Tf1 particles. We tested whether the putative Gag of Tf1 was required for particle formation, packaging of RNA, and reverse transcription. We generated deletions of 10 amino acids in each of the four hydrophilic domains of the protein and found that all four mutations reduced transposition activity. The N-terminal deletion removed a nuclear localization signal and inhibited nuclear import of the transposon. The two mutations in the center of Gag destabilized the protein and resulted in no virus-like particles. The C-terminal deletion caused a defect in RNA packaging and, as a result, low levels of cDNA. The electron microscopy of cells expressing a truncated Tf1 showed that Gag alone was sufficient for the formation of virus-like particles. Taken together, these results indicate that Tf1 encodes a Gag protein that is a functional equivalent of the Gag proteins of retroviruses.
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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.