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The Journal of Medical Microbiology, Vol 35, Issue 4 214-218, Copyright © 1991 by Society for General Microbiology
JOURNAL ARTICLE |
B. A. Wylie and H. J. Koornhof
Emergent Pathogen Unit, Medical Research Council, University of the Witwatersrand, Johannesburg, South Africa.
The complete sequence of the type VI dihydrofolate reductase (DHFR) gene from plasmid pUK672 was determined. The structural gene coded for a polypeptide of 157 amino acids which had a deduced mol. wt of 17,424. Comparison with amino-acid sequences of the type I, type V and Escherichia coli K12 chromosomal DHFRs showed that there was 63%, 61% and 31% homology respectively. Putative RNA polymerase and ribosomal binding sites were identified proximal to the initiation codon and a feature consistent with transcription termination was present distal to the coding region. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed that the enzyme had a subunit mol. wt of 17,500.
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