| Autor: |
Zywno‐van Ginkel, Sabrina, Dooley, Thomas P, Suling, William J, Barrow, William W |
| Zdroj: |
FEMS Microbiology Letters; November 1997, Vol. 156 Issue: 1 p69-78, 10p |
| Abstrakt: |
Dihydrofolate reductase is an essential bacterial enzyme necessary for the maintenance of intracellular folate pools in a biochemically active reduced state. In this report, the Mycobacterium avium folA gene was identified by functional genetic complementation, sequenced, and expressed for the first time. It has an open reading frame of 543 bp with a G+C content of 73%. The translated polypeptide sequence shows 58% identity to the consensus sequence of the conserved regions from eight other bacterial dihydrofolate reductases. Recombinant M. aviumdihydrofolate reductase was expressed actively in Escherichia coli, and SDS‐PAGE analysis revealed a 20 kDa species, agreeable with that predicted from the polypeptide sequence. |
| Databáze: |
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