The product of a newly identified gene, gInF, is required for synthesis of glutamine synthetase in Salmonella.
The product of a newly identified gene, glnF, which is distinct from the glutamine synthetase structural gene (glnA), is required for synthesis of glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2[ in Salmonella typhimurium and probably in Escherichia coli. Salmonella strains with ICR (2-chloro-6-methoxy-9-[3-(2-chloroethyl)aminopropylamino]acridine dihyodrochloride)-induced (frameshift) mutations in glnF are glutamine auxotrophs; they have less than 10% oof wild-type glutamine synthetase activity or antigen and are unable to derepress the synthesis of the enzyme. The mutant allele is recessive to the wild-type allele, indicating that the glnF gene encodes a diffusible product. Mutant glnF strains have normal activities of all proteins involved in covalent modification of glutamine synthetase: adenylyltransferase (EC 2.7.7.42), PII, uridylyltransferase, and uridylyl removing enzyme. In addition, they have glutamate synthase (EC 1.4.1.13) and glutamate dehydrogenase (EC 1.4.1.4) activities. Thus, glnF does not encode the structure of any of these proteins. The above evidence suggests that the product of the glnF gene is (or produces) a positive regulatory factor that is required for synthesis of glutamine synthetase; it indicates that auto-regulation cannot account for control of the synthesis of glutamine synthetase in Salmonella.
The product of a newly identified gene, gInF, is required for synthesis of glutamine synthetase in Salmonella. The product of a newly identified gene, glnF, which is distinct from the glutamine synthetase structural gene (glnA), is required for synthesis of glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2[ in Salmonella typhimurium and probably in Escherichia coli. Salmonella strains with ICR (2-chloro-6-methoxy-9-[3-(2-chloroethyl)aminopropylamino]acridine dihyodrochloride)-induced (frameshift) mutations in glnF are glutamine auxotrophs; they have less than 10% oof wild-type glutamine synthetase activity or antigen and are unable to derepress the synthesis of the enzyme. The mutant allele is recessive to the wild-type allele, indicating that the glnF gene encodes a diffusible product. Mutant glnF strains have normal activities of all proteins involved in covalent modification of glutamine synthetase: adenylyltransferase (EC 2.7.7.42), PII, uridylyltransferase, and uridylyl removing enzyme. In addition, they have glutamate synthase (EC 1.4.1.13) and glutamate dehydrogenase (EC 1.4.1.4) activities. Thus, glnF does not encode the structure of any of these proteins. The above evidence suggests that the product of the glnF gene is (or produces) a positive regulatory factor that is required for synthesis of glutamine synthetase; it indicates that auto-regulation cannot account for control of the synthesis of glutamine synthetase in Salmonella.