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
Regulatedin vitro synthesis of the enzymes of thedeo operon ofEscerichia coli
β Scribed by Svenningsen, Bo Ahlquist
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 924 KB
- Volume
- 137
- Category
- Article
- ISSN
- 0026-8925
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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
The infection of E. coli cells with different lambdoΓ―d prophages triggers a stimulation of galactokinase synthesis when cells are grown in a medium giving rise to a mild catabolite repression (tryptone broth) with an inducer of the gal operon (fucose). These results show that during phage infection