ArticleMolecular and cellular biology1998
Posttranslational regulation of Ty1 retrotransposition by mitogen-activated protein kinase Fus3.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 35 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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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Modulators of MAPK pathway activity during filamentous growth in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2024Article
- Article
- Reliance of Host-Encoded Regulators of Retromobility on Ty1 Promoter Activity or Architecture.Frontiers in molecular biosciences · 2022Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- Diverse transposable element landscapes in pathogenic and nonpathogenic yeast models: the value of a comparative perspective.Mobile DNA · 2020Review
- The Mediator co-activator complex regulates Ty1 retromobility by controlling the balance between Ty1i and Ty1 promoters.PLoS genetics · 2018Article
- Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.PLoS genetics · 2017Article
- Article
- The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.PLoS genetics · 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
- 5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition.Journal of virology · 2010Article
- Downregulation of Cdc2/CDK1 kinase activity induces the synthesis of noninfectious human papillomavirus type 31b virions in organotypic tissues exposed to benzo[a]pyrene.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
- Posttranslational interference of Ty1 retrotransposition by antisense RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- A Mep2-dependent transcriptional profile links permease function to gene expression during pseudohyphal growth in Saccharomyces cerevisiae.Molecular biology of the cell · 2008Article
- Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesis.Genetics · 2008Article
- S-phase checkpoint pathways stimulate the mobility of the retrovirus-like transposon Ty1.Molecular and cellular biology · 2007Article
- Host factors that control long terminal repeat retrotransposons in Saccharomyces cerevisiae: implications for regulation of mammalian retroviruses.Eukaryotic cell · 2007Review
- Severe adenine starvation activates Ty1 transcription and retrotransposition in Saccharomyces cerevisiae.Molecular and cellular biology · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Ty1 retrotransposons in Saccharomyces cerevisiae are maintained in a state of transpositional dormancy. We isolated a mutation, rtt100-1, that increases the transposition of genomic Ty1 elements 18- to 56-fold but has little effect on the transposition of related Ty2 elements. rtt100-1 was shown to be a null allele of the FUS3 gene, which encodes a haploid-specific mitogen-activated protein kinase. In fus3 mutants, the levels of Ty1 RNA, protein synthesis, and proteolytic processing were not altered relative to those in FUS3 strains but steady-state levels of TyA, integrase, and reverse transcriptase proteins and Ty1 cDNA were all increased. These findings suggest that Fus3 suppresses Ty1 transposition by destabilizing viruslike particle-associated proteins. The Fus3 kinase is activated through the mating-pheromone response pathway by phosphorylation at basal levels in naive cells and at enhanced levels in pheromone-treated cells. We demonstrate that suppression of Ty1 transposition in naive cells requires basal levels of Fus3 activation. Substitution of conserved amino acids required for activation of Fus3 derepressed Ty1 transposition. Moreover, epistasis analyses revealed that components of the pheromone response pathway that act upstream of Fus3, including Ste4, Ste5, Ste7, and Ste11, are required for the posttranslational suppression of Ty1 transposition by Fus3. The regulation of Ty1 transposition by Fus3 provides a haploid-specific mechanism through which environmental signals can modulate the levels of retrotransposition.
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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.