Regulation of enzyme synthesis by the glutamine synthetase of Salmonella typhimurium: a factor in addition to glutamine synthetase is required for activation of enzyme formation.
In Klebsiella aerogenes but not in Salmonella typhimurium glutamine synthetase can function during nitrogen-limited growth to increase the rate of synthesis of histidase from the hut genes of S. typhimurium 15-59 (hutS. 15-59). Formation of proline oxidase is also not increased in nitrogen-limited cultures of S. typhimurium. However, in hybrid strains of Escherichia coli or K. aerogenes, the glutamine synthetase of S. typhimurium activates synthesis of histidase from the hutS. 15-59 genes. Apparently, glutamine synthetase is necessary but not sufficient for activation of transcription of the hut genes; another factor must also be present. This factor is active in both K. aerogenes and E. coli but is missing or altered in S. typhimurium.
D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis; D004789:Enzyme Activation; D004798:Enzymes / Q000096:biosynthesis*; D004926:Escherichia coli / Q000201:enzymology; D005809:Genes, Regulator; D005838:Genotype; D005974:Glutamate-Ammonia Ligase / Q000096:biosynthesis / Q000378:metabolism*; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis; D007709:Klebsiella / Q000201:enzymology; D009584:Nitrogen / Q000494:pharmacology; D011392:Proline; D012486:Salmonella typhimurium / Q000201:enzymology*
D004798:Enzymes; D011392:Proline; D000594:Amino Acid Oxidoreductases; D006638:Histidine Ammonia-Lyase; D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen