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Expression of the tryptophan operon in merodiploids of Escherichia coli

✍ Scribed by Somerville, R. L. ;Stetson, H.

Publisher
Springer
Year
1974
Tongue
English
Weight
871 KB
Volume
131
Category
Article
ISSN
0026-8925

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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