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In vitro synthesis of enzymes of the tryptophan operon of Escherichia coli

โœ Scribed by Pouwels, P. H. ;van Rotterdam, J.

Publisher
Springer
Year
1975
Tongue
English
Weight
905 KB
Volume
136
Category
Article
ISSN
0026-8925

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โœฆ Synopsis

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 transcription, i.e. initiation and termination, is similar in vivo and in vitro.

๐Ÿ“œ SIMILAR VOLUMES

In vitro synthesis of enzymes of the try
In vitro synthesis of enzymes of the tryptophan operon of Escherichia coli
โœ Pouwels, P. H. ;van Rotterdam, J. ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Springer ๐ŸŒ English โš– 815 KB

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

Expression of Escherichia coli tryptopha
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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