ArticleJournal of virology2005
The long terminal repeat-containing retrotransposon Tf1 possesses amino acids in gag that regulate nuclear localization and particle formation.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Additional ORFs in Plant LTR-Retrotransposons.Frontiers in plant science · 2020Review
- Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.PLoS genetics · 2017Article
- The Long Terminal Repeat Retrotransposons Tf1 and Tf2 of Schizosaccharomyces pombe.Microbiology spectrum · 2015Review
- Nup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region.Molecular biology of the cell · 2015Article
- 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
- Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.PLoS pathogens · 2013Article
- The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid.Journal of virology · 2011Article
- Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins.Journal of virology · 2009Article
- The chromodomain of Tf1 integrase promotes binding to cDNA and mediates target site selection.Journal of virology · 2009Article
- 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
- New insights into the nuclear localization of retroviral Gag proteins.Nucleus (Austin, Tex.)Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Tf1 is a long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe that is studied to further our understanding of retrovirus propagation. One important application is to examine Tf1 as a model for how human immunodeficiency virus type 1 proteins enter the nucleus. The accumulation of Tf1 Gag in the nucleus requires an N-terminal nuclear localization signal (NLS) and the nuclear pore factor Nup124p. Here, we report that NLS activity is regulated by adjacent residues. Five mutant transposons were made, each with sequential tracts of four amino acids in Gag replaced by alanines. All five versions of Tf1 transposed with frequencies that were significantly lower than that of the wild type. Although all five made normal amounts of Gag, two of the mutations did not make cDNA, indicating that Gag contributed to reverse transcription. The localization of the Gag in the nucleus was significantly reduced by mutations A1, A2, and A3. These results identified residues in Gag that contribute to the function of the NLS. The Gags of A4 and A5 localized within the nucleus but exhibited severe defects in the formation of virus-like particles. Of particular interest was that the mutations in Gag-A4 and Gag-A5 caused their nuclear localization to become independent of Nup124p. These results suggested that Nup124p was only required for import of Tf1 Gag because of its extensive multimerization.
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