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Nucleic Acids Research, 1981, Vol. 9, No. 3 697-710
© 1981

Articles

Characterization of a R plasmid-associated, trimethoprim-resistant dihydrofolate reductase and determination of the nucleotide sequence of the reductase gene

J. Wemer Zolg and Urs J. Hänggi

Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie der Univeisität Goethestr. 33, 8000 München 2, GFR

Received November 17, 1980. The trimethoprim-resistant dihydrofolate reductase associated with the R plasmid R388 was isolated from strains that over-producethe enzyme. It was purified to apparent homogeneity by affinity chromatography and two consecutive gel filtration steps under native and denaturing conditions. The purified enzyme is composed of four identical subunits with molecular weights of 8300. A 1100 bp long DNA segment which confers resistance to trimethoprim was sequenced. The structural gene was identified on the plasmid DNA by comparing the amino acid composition of the deduced proteins with that of the purified enzyme. The gene is 234 bp long and codes for 78 amino acids. No homologycan be found between the deduced amino acid sequence of the R388 dihydrofolate reductase and those of other prokaryotic oreukaryotic dihydrofolate reductases. However, it differs in only 17 positions from the enzyme associated with the trimethoprim resistance plasmid R67.


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