## Background Dihydrofolate reductase (DHFR) and thymidylate synthase (TS) are crucial enzymes in DNA synthesis. In alveolata both enzymes are expressed as one bifunctional enzyme. ## Results Loss of this essential enzyme activities after successful allelic assortment of knock out alleles yields
Molecular cloning and analysis of a cDNA coding for the bifunctional dihydrofolate reductase-thymidylate synthase ofDaucus carota
โ Scribed by Meizhong Luo; Pietro Piffanelli; Luca Rastelli; Rino Cella
- Publisher
- Springer
- Year
- 1993
- Tongue
- English
- Weight
- 809 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0167-4412
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โฆ Synopsis
Molecular cloning of dihydrofolate reductase-thymidylate synthase (DHFR-TS) of Daucus carom was achieved by immunoscreening of a cDNA library obtaining a 2 kbp clone which contains an open reading frame of 1528 bp. Comparison of the deduced amino acid sequence with those from other sources revealed the presence of motifs typical of D H F R and TS thus confirming the bifunctional nature of the carrot protein. As in other organisms, a higher degree of conservation was observed in the TS domain. Analysis of the dhfr-ts gene content in carrot revealed the presence of several copies per diploid genome.
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