Polarity suppressors defective in transcription termination at the attenuator of the tryptophan operon of Escherichia coli have altered rho factor

Transcription termination factor rho purified from the polarity suppressor strains psu1, psu2 and psu4 is demonstrably different from wild-type rho. Rho factor from the mutant strains is more heat labile than wild-type rho. In addition, the ratio of transcription termination activity (Roberts, 1969)...

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Veröffentlicht in:	Journal of molecular biology 1976-09, Vol.106 (2), p.231-241
Hauptverfasser:	Korn, Laurence Jay, Yanofsky, Charles
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Anthranilate Synthase - metabolism Bacterial Proteins - metabolism Escherichia coli - metabolism Genes Kinetics Operon Peptide Termination Factors Species Specificity Suppression, Genetic Temperature Transcription, Genetic Tryptophan - biosynthesis Tryptophan Synthase - metabolism
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