PHYSIOLOGICAL PROPERTIES OF ARGININE SENSITIVE MUTANTS OF &lt;i&gt;SALMONELLA TYPHIMURIUM&lt;/i&gt;

Ishidsu, Jun-ichi

doi:10.1266/jjg.50.99

The Japanese journal of genetics

1975

DOI: 10.1266/jjg.50.99

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PHYSIOLOGICAL PROPERTIES OF ARGININE SENSITIVE MUTANTS OF <i>SALMONELLA TYPHIMURIUM</i>

Jun-ichi Ishidsu

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1976

1978

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Cited by 3 publications

(2 citation statements)

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“…Mutations leading to arginine sensitivity (ARS) were first reported by Ishidsu (9). The map position of the lesion (8), along with the low level of CPSase activity it confers (2), strongly suggests that the ARS phenotype results from certain mutations in pyrA, the structural gene encoding CPSase.…”

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Arginine-sensitive phenotype of mutations in pyrA of Salmonella typhimurium: role of ornithine carbamyltransferase in the assembly of mutant carbamylphosphate synthetase

Abdelal¹,

Griego²,

Ingraham³

1976

J Bacteriol

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The phenotype of certain mutations in pyrA, the gene encoding carbamylphosphate synthetase (CPSase), is expressed only in the presence od exogenous arginine. In unsupplemented media, synthesis of carbamylphosphate and growth was almost normal; in arginine-containing media, synthesis of carbamylphosphate stopped, as did growth, as a consequence of starvation for pyrimidine. Genetic and biochemical evidence suggests that arginine exerts this inhibition by repressing the synthesis of ornithine carbamyltransferase (OTCase), the intracellular presence of which is required for assembly of the unequal subunits and proper functioning of the mutant CPSase. After the addition of arginine to a culture of the mutant, CPSase activity (glutamine dependent) characteristic of the intact holoenzyme progressively decreased, whereas activity (ammonia dependent) characteristic of the free large (alpha) subunit increased. Extracts of mutant cells contain free small (beta) subunits, as demonstrated directly by in vitro complementation using purified alpha subunits from wild type. The mutant enzyme from cultures grown in the presence of arginine had a markedly decreased affinity for adenosine 5'-triphosphate. Mutations in argR that cause depressed synthesis of OTCase suppressed the phenotype, and a certain mutation in argI, the gene encoding OTCase, enhanced it. In vitro experiments using purified enzyme confirm the stimulatory effect of OTCase on the activity of mutant CPSase.

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confidence: 99%

Arginine-sensitive phenotype of mutations in pyrA of Salmonella typhimurium: role of ornithine carbamyltransferase in the assembly of mutant carbamylphosphate synthetase

Abdelal¹,

Griego²,

Ingraham³

1976

J Bacteriol

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“…pression of genetic inf ormations but their isolation is not easy as compared with the isolation of auxotrophs because of the lack of suitable selective media. In the case of arginine-sensitivity of Salmonella typhimurium, too, SJ1001 (ars-1, formerly arg-s-1) obtained from the wild strain LT2 (Ishidsu 1963(Ishidsu , 1964a(Ishidsu , 1964b has been the only one mutant so far isolated and detailed genetical analysis on this phenotype had to await the isolation of more mutants.…”

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confidence: 99%

DEVICE OF A METHOD FOR ISOLATION OF ARGININE SENSITIVE MUTANTS IN <i>SALMONELLA TYPHIMURIUM</i>

Ishidsu

1973

The Japanese journal of genetics

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Linkage map of Salmonella typhimurium, edition V

Sanderson¹,

Hartman²

1978

Microbiol Rev

126

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PHYSIOLOGICAL PROPERTIES OF ARGININE SENSITIVE MUTANTS OF <i>SALMONELLA TYPHIMURIUM</i>

Cited by 3 publications

References 34 publications

Arginine-sensitive phenotype of mutations in pyrA of Salmonella typhimurium: role of ornithine carbamyltransferase in the assembly of mutant carbamylphosphate synthetase

Arginine-sensitive phenotype of mutations in pyrA of Salmonella typhimurium: role of ornithine carbamyltransferase in the assembly of mutant carbamylphosphate synthetase

DEVICE OF A METHOD FOR ISOLATION OF ARGININE SENSITIVE MUTANTS IN <i>SALMONELLA TYPHIMURIUM</i>

Linkage map of Salmonella typhimurium, edition V

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