SUMMARY: A glutamine synthetase (GS) gene, , from was cloned on a recombinant plasmid pJS139 which enabled deletion mutants to utilize (NH)SO as a sole source of nitrogen. DNA homology was not detected between the gene and the gene. The cloned gene was expressed from its own promoter and was subject to nitrogen repression in , but it was not able to activate histidase activity in an deletion mutant containing the operon. The GS produced by pJS139 in was purified: it had an apparent subunit of approximately 75000, which is larger than that of any other known bacterial GS. There was very slight antigenic cross-reactivity between antibodies to the purified cloned GS and the GS subunit of wild-type


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