Mutations affecting glutamine synthetase activity in Salmonella typhimurium
نویسندگان
چکیده
منابع مشابه
Characterization of Salmonella typhimurium mutants with altered glutamine synthetase activity.
A number of glutamine auxotrophs of Salmonella typhimurium were isolated and characterized genetically. Three of the mutations appear to be closely linked and are complemented by episomes carrying the glnA region of Escherichia coli. The lesions in these strains are approximately 20% linked by P1 transduction with a mutation in the rha gene, but are unlinked to ilv. Another mutation causing glu...
متن کاملMutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium.
glnD and glnE mutant strains of Salmonella typhimurium lack three of the four activities required for reversible covalent modification of glutamine synthetase (GS; EC 6.3.1.2). The glnD strains, which are unable to deadenylylate GS and therefore accumulate the adenylylated or less active form of the enzyme, were isolated as glutamine bradytrophs. They lack the activity of PIIA uridylyl-transfer...
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Transcription of the genes for cobalamin biosynthesis is reduced during aerobic growth. We isolated and characterized mutants that showed a 2- to 90-fold increase in aerobic expression of the cobinamide biosynthesis (CobI) genes, depending on the particular mutation and growth conditions. Four different classes of mutations were characterized. All mutations (CobRI through CobRIV) were cis-actin...
متن کاملInteractions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium.
Glutamine synthetase (GS) catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia in the presence of divalent cations. To gain insight into the structural basis of the feedback inhibition of GS by AMP, we have studied crystal structures of GS complexes with AMP and the related molecules: AMPPNP (a less hydrolyzable ATP analog), ADP, GDP, adenosine, and adenine. AMP is a...
متن کاملL-Methionine SR-sulfoximine-resistant glutamine synthetase from mutants of Salmonella typhimurium.
Two mutants of Salmonella typhimurium resistant to growth inhibition by the glutamine synthetase transition state analog, L-methionine SR-sulfoximine, were isolated and characterized. These mutants are glutamine bradytrophs and cannot use growth rate-limiting nitrogen sources. Although this phenotype resembles that of mutants with lesions in the regulatory gene for glutamine synthetase, glnG, t...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1975
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.122.3.1006-1016.1975