ArticleMolecular & general genetics : MGG1987
Processing of TY1 proteins and formation of Ty1 virus-like particles in Saccharomyces cerevisiae.
Article in Molecular & general genetics : MGG, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 76 citations in OpenAlex.
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Article
- Retroviral-like determinants and functions required for dimerization of Ty1 retrotransposon RNA.RNA biology · 2019Article
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- BUD22 affects Ty1 retrotransposition and ribosome biogenesis in Saccharomyces cerevisiae.Genetics · 2010Article
- Mn2+ suppressor mutations and biochemical communication between Ty1 reverse transcriptase and RNase H domains.Journal of virology · 2007Article
- Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.Eukaryotic cell · 2005Article
- Ty1 defect in proteolysis at high temperature.Journal of virology · 2002Article
- A nucleocapsid functionality contained within the amino terminus of the Ty1 protease that is distinct and separable from proteolytic activity.Journal of virology · 2002Article
- Frameshift signal transplantation and the unambiguous analysis of mutations in the yeast retrotransposon Ty1 Gag-Pol overlap region.Journal of virology · 2001Article
- Characterization of a Sorghum bicolor gene family encoding putative protein kinases with a high similarity to the yeast SNF1 protein kinase.Plant molecular biology · 1998Article
- A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.Journal of virology · 1996Article
- Efficient homologous recombination of Ty1 element cDNA when integration is blocked.Molecular and cellular biology · 1994Article
- Ty1 in vitro integration: effects of mutations in cis and in trans.Molecular and cellular biology · 1994Article
- Reverse transcriptase activity of an intron encoded polypeptide.The EMBO journal · 1994Article
- Article
- A very poorly expressed tRNA(Ser) is highly concentrated together with replication primer initiator tRNA(Met) in the yeast Ty1 virus-like particles.Nucleic acids research · 1993Article
- Posttranslational control of Ty1 retrotransposition occurs at the level of protein processing.Molecular and cellular biology · 1992Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have analysed functional properties of putative proteins encoded by the yeast transposable element, Ty1, by overexpression of TY genes. High-level expression was achieved by appropriate fusion of a Ty sequence, TY9C, to the yeast ADH1 promoter and transformation of yeast cells with this construction. As shown recently by others (Garfinkel et al. 1985; Mellor et al. 1985c) TY overexpression leads to an increase in particle-bound reverse transcriptase activity and to an intracellular accumulation of virus-like particles (Ty-VLPs). We have used a number of deletions in the second open reading frame (TYB) to identify functional domains required for processing and assembly of Ty proteins. Deletions in the TYB region with homology to acid proteases result in overproduction of an unprocessed form of the TYA protein (pro-TYA) which represents the major protein of Ty-VLPs. One particular mutant construction, TY9C-delta 36, led to the accumulation of a particle-bound, 160 kDa protein which cross-reacted with a mouse antiserum raised against purified pro-TYA protein. This supports the hypothesis that TYB is expressed as a TYA/TYB fusion protein which is processed by a TYB-encoded protease activity. Ty-VLPs are formed in the absence of protein processing and even when the TYB gene is not expressed. Thus, we assume that the assembly of Ty particles occurs prior to processing of Ty proteins.
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