ArticleMolecular biotechnology2013
Prokaryotic expression and purification of soluble maize Ac transposase.
Article in Molecular biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Preparation of an anti-NEK2 monoclonal antibody and its application in liver cancer.BMC biotechnology · 2021Article
- Preparation of a novel monoclonal antibody against caprine interleukin-17A and its applications in immunofluorescence and immunohistochemistry assays.BMC biotechnology · 2019Article
- Redox-dependent interaction between thaumatin-like protein and β-glucan influences malting quality of barley.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Prokaryotic expression and purification of soluble goldfish Tgf2 transposase with transposition activity.Molecular biotechnology · 2015Article
- A root-specific wall-associated kinase gene, HvWAK1, regulates root growth and is highly divergent in barley and other cereals.Functional & integrative genomics · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transposons are mobile genetic elements that are found in all eukaryotic and prokaryotic species studied to date. The Maize Activator (Ac) transposase recognizes and excises Ac and Dissociation (Ds) elements and mediates insertion elsewhere in the genome. Insertions of Ds can cause disruption in gene sequences and hence are important functional genomics tool for tagging and cloning of unknown gene sequences. The involvement of Ac transposase (AcTPase) in Ds movement is well documented; however, protein structure and function of AcTPase is poorly understood. To express the maize AcTPase in E. coli, Ac cDNA was synthesized with an N-terminal 6xHis tag and cloned in pTrcAc expression vector. The expression cassette was induced in Rosetta2 (DE3) E. coli lines. End-point RT-PCR confirmed the integrity of AcTPase mRNA during cell culture. Autoinducing cultures grown at 37 °C produced prominent partial AcTPase products of ~40 kDa and ~70 kDa. Trypsin digestion and mass spectrometry analyses confirmed AcTPase in both the eluted peptides. When the cultures were grown at 22-25 °C for 24 h the expected ~90 kDa AcTPase soluble product was detected. The successful expression of full length AcTPase in soluble form allows further investigation of its structure and function.
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