Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties.

@article{Roth1966HistidineRM,
  title={Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties.},
  author={John R. Roth and Dora N. Ant{\'o}n and Philip E. Hartman},
  journal={Journal of molecular biology},
  year={1966},
  volume={22 2},
  pages={
          305-23
        }
}
View on PubMed
rothlab.ucdavis.edu
208 Citations
Highly Influential Citations
4
Background Citations
35
Methods Citations
7
Results Citations
1

Figures and Tables from this paper

208 Citations

Histidine regulatory mutants in Salmonella typhiumium. VI. Dominance studies.

Histidine regulatory mutants in Salmonella typhimurium. V. Two new classes histidine regulatory mutants.

  • D. Antón
  • Biology
    Journal of molecular biology
  • 1968

Histidine regulatory mutants in Salmonella typhimurium. IV. A positive selection for polar histidine-requiring mutants from histidine operator constitutive mutants.

Mutations creating a new initiation point for expression of the histidine operon in Salmonella typhimurium.

Genetic analysis of the histidine operon control region of Salmonella typhimurium.

Frameshift mutants in the histidine operon of Salmonella typhimurium.

  • R. Martin
  • Biology
    Journal of molecular biology
  • 1967

Biochemical and regulatory properties of Escherichia coli K-12 hisT mutants

The hisT mutants studied have a reduced growth rate that appears to be linked to hisT, although it is not known whether it is due to the same mutation.

Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase.

Catalytic defects in mutants of class II histidyl-tRNA synthetase from Salmonella typhimurium previously linked to decreased control of histidine biosynthesis regulation.

The kinetic analysis of five S. typhimurium bradytrophic mutants establishes a direct link between critical interactions within the active site of HisRS and regulation of histidine biosynthesis, and provides further evidence for the importance of local conformational changes during the catalytic cycle.

Mutations in the spoT gene of Salmonella typhimurium: effects on his operon expression

roximately 40% of these mutants are temperature sensitive for growth on minimal medium, suggesting that the spoT function is essential or that excessive accumulation of ppGpp is lethal.
...

References

SHOWING 1-10 OF 58 REFERENCES

Histidine regulatory mutants in Salmonella typhimurium. IV. A positive selection for polar histidine-requiring mutants from histidine operator constitutive mutants.

Frameshift mutants in the histidine operon of Salmonella typhimurium.

  • R. Martin
  • Biology
    Journal of molecular biology
  • 1967

The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium.

It has been found that the level of activity of the series of enzymes of Histidine biosynthesis can be raised about 15-fold over the wild-type level by growing a histidine-requiring mutant on formylhistidine as a source of histidine.

Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase.

Chromosomal alterations affecting the regulation of histidine biosynthetic enzymes in Salmonella.

Translation and polarity in the histidine operon. 3. The isolation of prototrophic polar mutations.

  • M. Voll
  • Biology
    Journal of molecular biology
  • 1967

MUTANTS OF SALMONELLA TYPHIMURIUM RESISTANT TO FEEDBACK INHIBITION BY L-HISTIDINE.

Under appropriate conditions, it should be possible to obtain mutants capable of producing an enzyme which is resistant to feedback inhibition but enzymatically active, and the possibility that such proteins have two distinct sites, a feedback inhibition site and an active site is suggested.

Heterogeneity in P22 transducing particles.

Histidine regulatory mutants in Salmonella typhimurium 3. A class of regulatory mutants deficient in tRNA for histidine.

Regulatory Mechanisms in the Biosynthesis of Isoleucine and Valine II. Identification of Two Operator Genes

Derepression of the condensing enzyme resulting from mutations in oprB confers resistance to low levels of valine, and to α-aminobutyric acid, and the significance of these findings with respect to the valine sensitivity of E. coli strain K-12 is discussed.
...