Mutant RNA polymerase of Escherichia coli terminates transcription in strains making defective rho factor.
We have isolated a rifampicin-resistant mutant of Escherichia coli RNA polymerase that restores transcription termination in strains with a defective rho protein. In such strains, the mutant RNA polymerase terminates transcription at normally rho-dependent sites at the end of the trp operon, in bacteriophage lambda, and within the lac operon. In addition, a strain with this mutant RNA polymerase remains viable with an amber mutation in rho, whereas a strain with wild-type RNA polymerase does not. These results suggest that the mutant RNA polymerase can terminate transcription at normally rho-dependent sites in the absence of rho.
D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D009154:Mutation; D009876:Operon; D010641:Phenotype; D012234:Rho Factor / Q000378:metabolism*; D012293:Rifampin / Q000494:pharmacology; D013696:Temperature; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic
D012234:Rho Factor; D014157:Transcription Factors; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin