Localization of the structural gene for threonine dehydrogenase in Escherichia coli
Open Access
- 30 September 1986
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 168 (1) , 434-436
- https://doi.org/10.1128/jb.168.1.434-436.1986
Abstract
The threonine dehydrogenase (tdh) gene of Escherichia coli, cloned within the plasmid pDR121, was inactivated in vitro by inserting a segment of DNA carrying the chloramphenicol acetyltransferase (cat) gene. The insertionally inactivated tdh gene was then transferred by homologous recombination into the E. coli chromosome by the procedure of Winans et al. (J. Bacteriol. 161:1219-1221, 1985). Mating experiments, followed by P1-mediated two- and three-point crosses, enabled us to localize tdh near min 81.2. The order with respect to known markers is mtl-cysE-tdh-pyrE.This publication has 29 references indexed in Scilit:
- ACETYLORNITHINASE OF ESCHERICHIA COLI: PARTIAL PURIFICATION AND SOME PROPERTIESPublished by Elsevier ,2021
- Linkage map of Escherichia coli K-12, edition 7.1983
- The plasmid cloning vector pBR325 contains a 482 base-pair-long inverted duplicationGene, 1981
- Construction and characterization of new cloning vehicles IV. Deletion derivatives of pBR322 and pBR325Gene, 1980
- Location of the Gene Specifying Hexose Phosphate Transport (uhp) on the Chromosome of Escherichia coliJournal of General Microbiology, 1977
- The frequency of P1 transduction of the genes of Escherichia coli as a function of chromosomal position: Preferential transduction of the origin of replicationMolecular Genetics and Genomics, 1977
- Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coliJournal of Bacteriology, 1976
- Novel mutants of Escherichia coli that accumulate very small DNA replicative intermediates.Proceedings of the National Academy of Sciences, 1975
- Genetic Recombination in Escherichia coli: The Role of Exonuclease IProceedings of the National Academy of Sciences, 1971
- Utilization of l-threonine by a species of Arthrobacter. A novel catabolic role for ‘aminoacetone synthase’Biochemical Journal, 1969