## Abstract Highly purified ribose‐binding protein from Escherichia coli has been used to reconstitute a binding‐protein‐dependent ribose transport in spheroplasts derived from a binding‐protein‐deficient mutant of E coli K 12, and in spheroplasts derived from Salmonella typhimurium. The cross‐spec
Cloning of the histidine transport genes from salmonella typhimurium and characterization of an analogous transport system in escherichia coli
✍ Scribed by Ardeshir, Feroza ;Ames, Giovanna Ferro-Luzzi
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1980
- Tongue
- English
- Weight
- 993 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The genes for the well‐characterized high‐affinity histidine transport system of S typhimurium have been cloned in λgt4. Genetic and physiological analyses of the analogous transport system of E coli were undertaken in order that available λ vectors, recombinant DNA techniques, and a genetic selection for transport function might be used to isolate the Salmonella genes. The presence of the transport genes on a 12.4 Kb cloned DNA fragment has been confirmed (1) genetically, by complementation studies; (2) physiologically, by the rates of histidine uptake by bacteria containing this DNA; and (3) by demonstrating that the cloned DNA codes for the previously identified transport proteins J and P. The isolated fragment carries the entire transport operon, the argT gene and the ubiX locus, but neither the purF gene nor the ack/pta loci.
📜 SIMILAR VOLUMES