Regulation of the tryptophan operon of Escherichia coli integrated into the phage ϕ80 genome
✍ Scribed by Inoko, Hidetoshi ;Naito, Shigetaka ;Ito, Koreaki ;Imai, Mutsuo
- Publisher
- Springer
- Year
- 1974
- Tongue
- English
- Weight
- 766 KB
- Volume
- 129
- Category
- Article
- ISSN
- 0026-8925
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The rate of synthesis and intracellular content of the NusA protein, a transcription termination factor, were determined for wild-type and nusA and/or nusB mutants of Escherichia coli. Both the rate and content of NusA in wild-type strains were similar to that of the RNA polymerase sigma subunit, a
In vitro synthesis of enzymes of the tryptophan (trp) operon of E. coli was studied in an extract prepared from E. coli, which is programmed with purified DNA from trp transducing phages with mutations that effect the expression of the trp genes in various ways. Our results show that control of tran
A protein fraction, called At (= anti termination) factor, has been isolated from extracts of E. coli and partially purified. The At factor stimulates the synthesis in vitro of anthranilate synthetase, an enzyme encoded by two genes of the tryptophan (trp) operon, but has no effect on the synthesis