ArticleThe Plant cell2001
The Arabidopsis TAG1 transposase has an N-terminal zinc finger DNA binding domain that recognizes distinct subterminal motifs.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
- Alternative plant host defense against transposon activities occurs at the post-translational stage.Plant signaling & behavior · 2017Article
- Detainment of Tam3 Transposase at Plasma Membrane by Its BED-Zinc Finger Domain.Plant physiology · 2017Article
- Biochemical Characterization of Kat1: a Domesticated hAT-Transposase that Induces DNA Hairpin Formation and MAT-Switching.Scientific reports · 2016Article
- Nitrate foraging by Arabidopsis roots is mediated by the transcription factor TCP20 through the systemic signaling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Soluble expression, purification and characterization of the full length IS2 Transposase.Mobile DNA · 2011Article
- DNA sequence requirements for hobo transposable element transposition in Drosophila melanogaster.Genetica · 2011Article
- DNA binding activities of the Herves transposase from the mosquito Anopheles gambiae.Mobile DNA · 2011Article
- Site specific cytosine methylation in rice nonautonomous transposable element nDart.Plant molecular biology · 2008Article
- The temperature-dependent change in methylation of the Antirrhinum transposon Tam3 is controlled by the activity of its transposase.The Plant cell · 2006Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The in vitro DNA binding activity of the Arabidopsis Tag1 transposase (TAG1) was characterized to determine the mechanism of DNA recognition. In addition to terminal inverted repeats, the Tag1 element contains four different subterminal repeats that flank a transcribed region encoding a 729-amino acid protein. A single site-specific DNA binding domain is located near the N terminus of TAG1, between residues 21 and 133. This domain binds specifically to the AAACCC and TGACCC subterminal repeats, found near the 5' and 3' ends of the element, respectively. The ACCC sequence within these repeats is critical for recognition because mutations at positions 3, 5, and 6 abolished binding, yet the first two bases also are important because substitutions at these positions decreased binding by up to 90%. Weak interaction also occurs with the terminal inverted repeats, but no binding was observed to the other two 3' subterminal repeat regions. Sequence analysis of the TAG1 DNA binding domain revealed a C(2)HC zinc finger motif. Tests for metal dependence showed that DNA binding activity was inhibited by divalent metal chelators and greatly enhanced by zinc. Furthermore, mutation of each cysteine residue predicted to be a metal ligand in the C(2)HC motif abolished DNA binding. Together, these data show that the DNA binding domain of TAG1 specifically binds to distinct subterminal repeats and contains a zinc finger.
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