Abstract
Two strains with mutations in the first structural gene of the histidine operon of Salmonella typhimurium were characterized. (The first structural gene specifies the first enzyme of histidine biosynthesis, phosphoribosyltransferase, which is sensitive to feedback inhibition by histidine.) One mutation, hisG3934, results in a phosphoribosyltransferase which is no longer sensitive to feedback inhibition by histidine but is instead subject to inhibition by aspartic acid. The other mutation, hisG3935, allows the histidine operon to be partially repressed by several amino acids, including aspartic acid. Analysis of hisG3935 is consistent with the hypothesis that phosphoribosyltransferase is directly involved in the regulation of the histidine operon.
MeSH Terms
Amino Acids/pharmacology
Aspartic Acid/metabolism,pharmacology
Chromosome Mapping
Culture Media
Drug Resistance, Microbial
Enzyme Repression
Genes
Genetics, Microbial
Histidine/metabolism,pharmacology
Microbial Sensitivity Tests
Models, Theoretical
Molecular Biology
Mutation
Operon
Paper
Phosphotransferases/antagonists & inhibitors,metabolism
Recombination, Genetic
Salmonella typhimurium/drug effects,enzymology,growth & development,isolation & purification,metabolism
Spectrophotometry
Transduction, Genetic
Triazoles
Chemicals
Amino Acids
Culture Media
Triazoles
Aspartic Acid
Histidine
Phosphotransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rothman-Denes L
Martin R G
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