Genetic Mapping of Loci for Glucose-6-Phosphate Dehydrogenase, Gluconate-6-Phosphate Dehydrogenase, and Gluconate-6-Phosphate Dehydrase in Escherichia coli
- 1 April 1968
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 95 (4) , 1272-+
- https://doi.org/10.1128/jb.95.4.1272-1278.1968
Abstract
The loci on the Escherichia coli genome of mutations affecting the constitutive enzymes glucose-6-phosphate dehydrogenase ( zwf ) and gluconate-6-phosphate dehydrogenase ( gnd ), and the inducible enzyme gluconate-6-phosphate dehydrase ( edd ), were determined by conjugation and transduction experiments, chiefly by three-factor crosses. They are in the same region of the chromosome, and their order is gnd—his— ( edd, zwf ) —aroD; gnd and his are cotransduceable, as are zwf and edd . The position of gnd in Salmonella typhimurium was shown to be similar to that in E. coli .This publication has 23 references indexed in Scilit:
- Selection of Escherichia coli Mutants Lacking Glucose-6-Phosphate Dehydrogenase or Gluconate-6-Phosphate DehydrogenaseJournal of Bacteriology, 1968
- Extended deletions in the histidine-rough-B region of the Salmonella chromosome.Proceedings of the National Academy of Sciences, 1967
- Location on the chromosome of Escherichia coli of a gene specifying phosphopyruvate synthase activityBiochimica et Biophysica Acta (BBA) - General Subjects, 1967
- Gluconate Metabolism in Escherichia coliJournal of Bacteriology, 1967
- Histidine regulatory mutants in Salmonella typhimuriumJournal of Molecular Biology, 1966
- Low recombination frequency for markers very near the origin in conjugation inE. coliGenetics Research, 1965
- ISOLATION AND CHARACTERIZATION OF RECOMBINATION-DEFICIENT MUTANTS OF ESCHERICHIA COLI K12Proceedings of the National Academy of Sciences, 1965
- GENES AND PROTEINS INVOLVED IN HISTIDINE BIOSYNTHESIS IN SALMONELLA.1964
- F' and F Mediated Transduction in Escherichia coli K12The Japanese Journal of Genetics, 1961
- On the physical state of the intracellularly accumulated substrates of β-galactoside-permease in Escherichia coliBiochimica et Biophysica Acta, 1958