Effect of dnaA and rpoB mutations on attenuation in the trp operon of Escherichia coli.
The rate of synthesis of tryptophan synthetase was found to be increased by heat inactivation of the dnaA protein in three dnaA mutants temperature sensitive for initiation of DNA replication. The effect of the dnaA mutations was dependent upon the presence of an intact attenuator in the tryptophan operon. The activity of the mutated dnaA protein at the tryptophan attenuator and its activity as initiator for chromosome replication decreased gradually with increasing temperature. Two rpoB mutations that suppress the temperature defect of the dnaA46 mutation in initiation of replication were tested for effects on attenuation in the tryptophan operon. One of the rpoB mutations caused increased transcription termination at the attenuator independent of the dnaA allele, whereas the other mutation had no effect. Expression of the histidine and threonine operons, which are also regulated by attenuation, was unaffected by the dnaA mutations.
D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D005798:Genes, Bacterial; D006642:Histidinol-Phosphatase / Q000096:biosynthesis; D006715:Homoserine Dehydrogenase / Q000096:biosynthesis; D009154:Mutation; D009876:Operon; D013489:Suppression, Genetic; D013696:Temperature; D014158:Transcription, Genetic; D014364:Tryptophan / Q000096:biosynthesis*; D014367:Tryptophan Synthase / Q000096:biosynthesis
D001426:Bacterial Proteins; D014364:Tryptophan; D006715:Homoserine Dehydrogenase; D006642:Histidinol-Phosphatase; D014367:Tryptophan Synthase