Abstract
The glutamine synthetase (GS) gene glnA of Thiobacillus ferrooxidans was cloned on recombinant plasmid pMEB100 which enabled Escherichia coli glnA deletion mutants to utilize (NH4)2SO4 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.
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- Alvarez-Morales A., Dixon R., Merrick M. Positive and negative control of the glnA ntrBC regulon in Klebsiella pneumoniae. EMBO J. 1984 Mar;3(3):501–507. doi: 10.1002/j.1460-2075.1984.tb01837.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Backman K., Chen Y. M., Magasanik B. Physical and genetic characterization of the glnA--glnG region of the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3743–3747. doi: 10.1073/pnas.78.6.3743. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barros M. E., Rawlings D. E., Woods D. R. Mixotrophic Growth of a Thiobacillus ferrooxidans Strain. Appl Environ Microbiol. 1984 Mar;47(3):593–595. doi: 10.1128/aem.47.3.593-595.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bender R. A., Janssen K. A., Resnick A. D., Blumenberg M., Foor F., Magasanik B. Biochemical parameters of glutamine synthetase from Klebsiella aerogenes. J Bacteriol. 1977 Feb;129(2):1001–1009. doi: 10.1128/jb.129.2.1001-1009.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Dagert M., Ehrlich S. D. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene. 1979 May;6(1):23–28. doi: 10.1016/0378-1119(79)90082-9. [DOI] [PubMed] [Google Scholar]
- Garcia E., Bancroft S., Rhee S. G., Kustu S. The product of a newly identified gene, gInF, is required for synthesis of glutamine synthetase in Salmonella. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1662–1666. doi: 10.1073/pnas.74.4.1662. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ish-Horowicz D., Burke J. F. Rapid and efficient cosmid cloning. Nucleic Acids Res. 1981 Jul 10;9(13):2989–2998. doi: 10.1093/nar/9.13.2989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kustu S. G., McFarland N. C., Hui S. P., Esmon B., Ames G. F. Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. J Bacteriol. 1979 Apr;138(1):218–234. doi: 10.1128/jb.138.1.218-234.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Magasanik B. Genetic control of nitrogen assimilation in bacteria. Annu Rev Genet. 1982;16:135–168. doi: 10.1146/annurev.ge.16.120182.001031. [DOI] [PubMed] [Google Scholar]
- McFarland N., McCarter L., Artz S., Kustu S. Nitrogen regulatory locus "glnR" of enteric bacteria is composed of cistrons ntrB and ntrC: identification of their protein products. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2135–2139. doi: 10.1073/pnas.78.4.2135. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pahel G., Tyler B. A new glnA-linked regulatory gene for glutamine synthetase in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4544–4548. doi: 10.1073/pnas.76.9.4544. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rawlings D. E., Woods D. R. Mobilization of Thiobacillus ferrooxidans plasmids among Escherichia coli strains. Appl Environ Microbiol. 1985 May;49(5):1323–1325. doi: 10.1128/aem.49.5.1323-1325.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SILVERMAN M. P., LUNDGREN D. G. Studies on the chemoautotrophic iron bacterium Ferrobacillus ferrooxidans. I. An improved medium and a harvesting procedure for securing high cell yields. J Bacteriol. 1959 May;77(5):642–647. doi: 10.1128/jb.77.5.642-647.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith G. E., Summers M. D. The bidirectional transfer of DNA and RNA to nitrocellulose or diazobenzyloxymethyl-paper. Anal Biochem. 1980 Nov 15;109(1):123–129. doi: 10.1016/0003-2697(80)90019-6. [DOI] [PubMed] [Google Scholar]
- Smith G. R., Halpern Y. S., Magasanik B. Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase. J Biol Chem. 1971 May 25;246(10):3320–3329. [PubMed] [Google Scholar]
- Tuli R., Fisher R., Haselkorn R. The ntr genes of Escherichia coli activate the hut and nif operons of Klebsiella pneumoniae. Gene. 1982 Jul-Aug;19(1):109–116. doi: 10.1016/0378-1119(82)90195-0. [DOI] [PubMed] [Google Scholar]
- Tuovinen O. H., Panda F. A., Tsuchiya H. M. Nitrogen requirement of iron-oxidizing thiobacilli for acidic ferric sulfate regeneration. Appl Environ Microbiol. 1979 May;37(5):954–958. doi: 10.1128/aem.37.5.954-958.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tyler B. Regulation of the assimilation of nitrogen compounds. Annu Rev Biochem. 1978;47:1127–1162. doi: 10.1146/annurev.bi.47.070178.005403. [DOI] [PubMed] [Google Scholar]

