ArticleJournal of bacteriology2007
Site-directed mutagenesis studies of tn5 transposase residues involved in synaptic complex formation.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 8 citations in OpenAlex.
- OpenTn5: Open-Source Resource for Robust and Scalable Tn5 Transposase Purification and Characterization.bioRxiv : the preprint server for biology · 2024Article
- Transposase-assisted tagmentation: an economical and scalable strategy for single-worm whole-genome sequencing.G3 (Bethesda, Md.) · 2024Article
- Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy.Biochemistry · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Transposition (the movement of discrete segments of DNA, resulting in rearrangement of genomic DNA) initiates when transposase forms a dimeric DNA-protein synaptic complex with transposon DNA end sequences. The synaptic complex is a prerequisite for catalytic reactions that occur during the transposition process. The transposase-DNA interactions involved in the synaptic complex have been of great interest. Here we undertook a study to verify the protein-DNA interactions that lead to synapsis in the Tn5 system. Specifically, we studied (i) Arg342, Glu344, and Asn348 and (ii) Ser438, Lys439, and Ser445, which, based on the previously published cocrystal structure of Tn5 transposase bound to a precleaved transposon end sequence, make cis and trans contacts with transposon end sequence DNA, respectively. By using genetic and biochemical assays, we showed that in all cases except one, each of these residues plays an important role in synaptic complex formation, as predicted by the cocrystal structure.
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Registered trials
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