ArticleMolecular and cellular biology1992
Posttranslational control of Ty1 retrotransposition occurs at the level of protein processing.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 72 citations in OpenAlex.
- A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition.Mobile DNA · 2022Article
- Reliance of Host-Encoded Regulators of Retromobility on Ty1 Promoter Activity or Architecture.Frontiers in molecular biosciences · 2022Article
- Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families.Current genetics · 2021Review
- Saccharomyces cerevisiae RNA lariat debranching enzyme, Dbr1p, is required for completion of reverse transcription by the retrovirus-like element Ty1 and cleaves branched Ty1 RNAs.Molecular genetics and genomics : MGG · 2021Article
- Transposable Element Mobilization in Interspecific Yeast Hybrids.Genome biology and evolution · 2021Article
- A small targeting domain in Ty1 integrase is sufficient to direct retrotransposon integration upstream of tRNA genes.The EMBO journal · 2020Article
- Article
- Ribosome Biogenesis Modulates Ty1 Copy Number Control inGenetics · 2017Article
- A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces.Current genetics · 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
- A trans-dominant form of Gag restricts Ty1 retrotransposition and mediates copy number control.Journal of virology · 2015Article
- The Ty1 LTR-retrotransposon of budding yeast,Microbiology spectrum · 2015Article
- A role for the budding yeast separase, Esp1, in Ty1 element retrotransposition.PLoS genetics · 2015Article
- Retrotransposon Ty1 RNA contains a 5'-terminal long-range pseudoknot required for efficient reverse transcription.RNA (New York, N.Y.) · 2013Article
- Ty1 gag enhances the stability and nuclear export of Ty1 mRNA.Traffic (Copenhagen, Denmark) · 2013Article
- Catalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1.PloS one · 2013Article
- Host co-factors of the retrovirus-like transposon Ty1.Mobile DNA · 2012Article
- 5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition.Journal of virology · 2010Article
- P-body components are required for Ty1 retrotransposition during assembly of retrotransposition-competent virus-like particles.Molecular and cellular biology · 2010Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
High-level expression of a transpositionally competent Ty1 element fused to the inducible GAL1 promoter on a 2 microns plasmid (pGTy1) overcomes transpositional dormancy in Saccharomyces cerevisiae. To investigate the mechanisms controlling the rate of Ty1 retrotransposition, we quantitated transposition and Ty1 gene products in cells induced and uninduced for expression of pGTy1. The increase in Ty1 transposition was 45- to 125-fold greater than the increase in Ty1 RNA effected by pGTy1 induction. Translational efficiency of Ty1 RNA was not altered in transposition-induced cells, since p190TYA1-TYB1 protein synthesis increased in proportion to steady-state Ty1 RNA levels. Therefore, expression of a pGTy1 element increases the efficiency of Ty1 transposition at a posttranslational level. Galactose induction of pGTy1 enhanced TYA1 protein processing and allowed detection of processed TYB1 proteins, which are normally present at very low levels in uninduced cells. When the ability of genomic Ty1 elements to complement defined mutations in HIS3-marked pGTy1 elements was examined, mutations in the protease domain or certain mutations in the integrase domain failed to be complemented, but mutations in the reverse transcriptase domain were partially complemented by genomic Ty1 elements. Therefore, the activity of Ty1 elements in yeast cells may be limited by the availability of Ty1 protease and possibly integrase. These results suggest that Ty1 transposition is regulated at the level of protein processing and that this regulation is overcome by expression of a pGTy1 element.
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