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Cloning and expression of the Thiobacillus ferrooxidans glutamine synthetase gene in Escherichia coli

Journal Article · · J. Bacteriol.; (United States)
OSTI ID:5392833

The glutamine synthetase (GS) gene glnA of Thiobacillus ferrooxidans was cloned on recombinant plasmid pMEB100 which enabled Escherichia coli glnA deletion mutants to utilize (NH/sub 4/)/sub 2/SO/sub 4/ as the sole source of nitrogen. High levels of GS-specific activity were obtained in the E. coli glnA deletion mutants containing the T. ferrooxidans GS gene. The cloned T. ferrooxidans DNA fragment containing the glnA gene activated histidase activity in an E. coli glnA glnL glnG deletion mutant containing the Klebsiella aerogenes hut operon. Plasmid pMEB100 also enabled the E. coli glnA glnL glnG deletion mutant to utilize arginine or low levels of glutamine as the sole source of nitrogen. There was no detectable DNA homology between the T. ferrooxidans glnA gene and the E. coli glnA gene.

Research Organization:
Univ. of Cape Town, Rondebosch, South Africa
OSTI ID:
5392833
Journal Information:
J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 164:3; ISSN JOBAA
Country of Publication:
United States
Language:
English