ArticleBMC biotechnology2006
The bifunctional dihydrofolate reductase thymidylate synthase of Tetrahymena thermophila provides a tool for molecular and biotechnology applications.
Article in BMC biotechnology, 2006. 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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3 citing papers in PubMed, 10 citations in OpenAlex.
- A recombinase system facilitates cloning of expression cassettes in the ciliate Tetrahymena thermophila.BMC microbiology · 2007Article
- Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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5 authors at 2 institutions in 1 country.
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Abstract
backgroundDihydrofolate reductase (DHFR) and thymidylate synthase (TS) are crucial enzymes in DNA synthesis. In alveolata both enzymes are expressed as one bifunctional enzyme.
resultsLoss of this essential enzyme activities after successful allelic assortment of knock out alleles yields an auxotrophic marker in ciliates. Here the cloning, characterisation and functional analysis of Tetrahymena thermophila's DHFR-TS is presented. A first aspect of the presented work relates to destruction of DHFR-TS enzyme function in an alveolate thereby causing an auxotrophy for thymidine. A second aspect is to knock in an expression cassette encoding for a foreign gene with subsequent expression of the target protein.
conclusionThis system avoids the use of antibiotics or other drugs and therefore is of high interest for biotechnological applications.
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