Regulation of histidine operon does not require hisG enzyme.
- 1 December 1975
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (12) , 5021-5025
- https://doi.org/10.1073/pnas.72.12.5021
Abstract
Mutations are described which delete all or part of the first structural gene (hisG) of the histidine operon of Salmonella typhimurium. Physiological regulation of histidine enzymes occurs normally in strains carrying any deletion that has both endpoints within the hisG gene. Constitutive high operon expression is observed in strains carrying any hisG deletion and an unlinked regulatory mutation, hisT1504. These results strongly indicate that the hisG protein is not an essential component of the mechanism for regulating expression of the histidine operon.Keywords
This publication has 22 references indexed in Scilit:
- Regulation of isoleucine-valine biosynthesis in an ilvDAC deletion strain of Escherichia coli K-12Biochemical and Biophysical Research Communications, 1974
- Autogenous Regulation of Gene ExpressionScience, 1974
- Internal deletions in the tryptophan operon of Escherichia coliJournal of Molecular Biology, 1972
- Overproduction of hisH and hisF gene products leads to inhibition of cell division in SalmonellaCanadian Journal of Microbiology, 1972
- Histidine regulatory mutants in Salmonella typhimuriumJournal of Molecular Biology, 1968
- Histidine regulatory mutants in salmonella typhimuriumJournal of Molecular Biology, 1967
- A phage P22 gene controlling integration of prophageVirology, 1967
- Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): Inhibition of an enzyme of histidine biosynthesisArchives of Biochemistry and Biophysics, 1965
- Heterogeneity in P22 transducing particlesVirology, 1965
- Fine Structure Mapping by Complete Transduction Between Histidine-requiring Salmonella MutantsJournal of General Microbiology, 1960