ArticleJournal of virology1996
A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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.
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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
38 citing papers in PubMed.
- An interchangeable prion-like domain is required for Ty1 retrotransposition.bioRxiv : the preprint server for biology · 2023Article
- 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
- Article
- The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.Retrovirology · 2018Article
- Retrotransposon targeting to RNA polymerase III-transcribed genes.Mobile DNA · 2018Review
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.PLoS genetics · 2015Article
- Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions.Nucleic acids research · 2015Article
- The Ty1 LTR-retrotransposon of budding yeast,Microbiology spectrum · 2015Article
- Ribosomal protein and biogenesis factors affect multiple steps during movement of the Saccharomyces cerevisiae Ty1 retrotransposon.Mobile DNA · 2015Article
- BUD22 affects Ty1 retrotransposition and ribosome biogenesis in Saccharomyces cerevisiae.Genetics · 2010Article
- Article
- Nucleocapsid protein function in early infection processes.Virus research · 2008Review
- S-phase checkpoint pathways stimulate the mobility of the retrovirus-like transposon Ty1.Molecular and cellular biology · 2007Article
- Cooperation between reverse transcriptase and integrase during reverse transcription and formation of the preintegrative complex of Ty1.Eukaryotic cell · 2006Article
- Characterization of a nucleocapsid-like region and of two distinct primer tRNALys,2 binding sites in the endogenous retrovirus Gypsy.Nucleic acids research · 2006Article
- Investigation by atomic force microscopy of the structure of Ty3 retrotransposon particles.Journal of virology · 2005Article
- Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.Eukaryotic cell · 2005Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Cleavage of the Gag and Gag-Pol polyprotein precursors is a critical step in proliferation of retroviruses and retroelements. The Ty1 retroelement of Saccharomyces cerevisiae forms virus-like particles (VLPs) made of the Gag protein. Ty1 Gag is not obviously homologous to the Gag proteins of retroviruses. The apparent molecular mass of Gag is reduced from 58 to 54 kDa during particle maturation. Antibodies raised against the C-terminal peptide of Gag react with the 58-kDa polypeptide but not with the 54-kDa one, indicating that Gag is proteolytically processed at the C terminus. A protease cleavage site between positions 401 and 402 of the Gag precursor was defined by carboxy-terminal sequencing of the processed form of Gag. Certain deletion and substitution mutations in the C terminus of the Gag precursor result in particles that are two-thirds the diameter of the wild-type VLPs. While the Ty1 protease is active in these mutants, their transposition rates are decreased 20-fold compared with that of wild-type Ty1. Thus, the Gag C-terminal portion, released in the course of particle maturation, probably plays a significant role in VLP morphogenesis and Ty1 transposition.
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Registered trials
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