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PMID: 4928009 Published · ppublish English Journal Article

Two mutations in the first gene of the histidine operon of Salmonella typhimurium affecting control.

Journal of bacteriology ·Vol. 106 ·No. 1 ·1971-04-00 ·Pages 227-37

Rothman-Denes L, Martin RG

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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24 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1971-04-00
Pages
227-37
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC248666
Subset
IM
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