ArticlePloS one2011
Nuclear importation of Mariner transposases among eukaryotes: motif requirements and homo-protein interactions.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- ThebioRxiv : the preprint server for biology · 2025Article
- Characterization of Mariner transposons in seven species of Rhus gall aphids.Scientific reports · 2021Article
- The C-terminal Domain of piggyBac Transposase Is Not Required for DNA Transposition.Journal of molecular biology · 2021Article
- Nuclear export signal (NES) of transposases affects the transposition activity of mariner-like elementsMobile DNA · 2019Article
- Mariner Transposons Contain a Silencer: Possible Role of the Polycomb Repressive Complex 2.PLoS genetics · 2016Article
- cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses.Nucleic acids research · 2014Article
- Reliability of the nanopheres-DNA immunization technology to produce polyclonal antibodies directed against human neogenic proteins.Molecular genetics and genomics : MGG · 2013Article
- Article
- The emerging diversity of transpososome architectures.Quarterly reviews of biophysics · 2012Review
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Authors and funding
11 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mariner-like elements (MLEs) are widespread transposable elements in animal genomes. They have been divided into at least five sub-families with differing host ranges. We investigated whether the ability of transposases encoded by Mos1, Himar1 and Mcmar1 to be actively imported into nuclei varies between host belonging to different eukaryotic taxa. Our findings demonstrate that nuclear importation could restrict the host range of some MLEs in certain eukaryotic lineages, depending on their expression level. We then focused on the nuclear localization signal (NLS) in these proteins, and showed that the first 175 N-terminal residues in the three transposases were required for nuclear importation. We found that two components are involved in the nuclear importation of the Mos1 transposase: an SV40 NLS-like motif (position: aa 168 to 174), and a dimerization sub-domain located within the first 80 residues. Sequence analyses revealed that the dimerization moiety is conserved among MLE transposases, but the Himar1 and Mcmar1 transposases do not contain any conserved NLS motif. This suggests that other NLS-like motifs must intervene in these proteins. Finally, we showed that the over-expression of the Mos1 transposase prevents its nuclear importation in HeLa cells, due to the assembly of transposase aggregates in the cytoplasm.
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