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Expression of Escherichia coli tryptophan operon in Rhizobium leguminosarum

✍ Scribed by Nagahari, Kenji ;Koshikawa, Takako ;Sakaguchi, Kenji

Publisher
Springer
Year
1979
Tongue
English
Weight
394 KB
Volume
171
Category
Article
ISSN
0026-8925

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✦ Synopsis

RP4-trp hybrid plasmid containing Escherichia coli whole tryptophan operon was conjugatively transferred from E. coli to Rhizobium leguminosarum strains carrying mutations in different trp genes, converting their Trp- phenotype to Trp+. That the phenotype change of the R. leguminosarum cells was due to the presence of the E. coli tryptophan operon was verified by the isolation of RP4-trp hybrid plasmid from the R. leguminosarum conjugant cells, and by re-transfer of RP4-trp plasmid by conjugation back to E. coli trp and Pseudomonas putida trp strains. Enzymatic activities of anthranilate synthetase and beta subunit of tryptophan synthetase in crude extracts of R. leguminosarum cells containing RP4-trp plasmid were much higher than that of the wild-type cells and were not repressed by the presence of tryptophan in the culture medium.

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In vitro synthesis of enzymes of the try
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✍ Pouwels, P. H. ;van Rotterdam, J. πŸ“‚ Article πŸ“… 1975 πŸ› Springer 🌐 English βš– 905 KB

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

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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