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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
815 KB
Volume
136
Category
Article
ISSN
0026-8925

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โœฆ Synopsis

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 of T7 RNA polymerase and other T7- and T4 coded proteins. The At factor stimulates the synthesis of trp mRNA; it has no effect on the translation of trp mRNA. We conclude that in vitro transcription of the trp operon is positively controlled.

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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– 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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