Abstract
Mutations at two sites of the Klebsiella aerogenes chromosome, unlinked by transduction with phages PW52 and P1, result in the lack of enzymatically active glutamine synthetase. A mutation in the glnB site leads to a marked decrease in the formation of an apparently normal enzyme. Some of the mutations in the glnA site lead to the production of enzymatically inactive material capable of reacting with anti-glutamine synthetase serum. The revertant of a glnA mutant was found to produce a glutamine synthetase with less activity and less stability to heat than the enzyme of the wild type. These results locate the structural gene to the production of enzymatically inactive glutamine synthetase antigen, not subject to repression by exogenously added ammonia. This observation suggests that glutamine synthetase is itself involved in the regulation of the synthesis of glutamine synthetase.
MeSH Terms
Ammonia/metabolism
Antigens, Bacterial/analysis
Cell-Free System
Chemical Precipitation
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Genes
Glutamate-Ammonia Ligase/biosynthesis,immunology,metabolism
Glutamine/metabolism
Hot Temperature
Klebsiella/enzymology,growth & development,metabolism
Mutation
Transduction, Genetic
Zinc
Chemicals
Antigens, Bacterial
Glutamine
Ammonia
Glutamate-Ammonia Ligase
Zinc
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Deleo A B
Magasanik B
References (10)
10 references, click to expand
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