Transcription termination factor rho from wild type and rho-111 strains of Salmonella typhimurium.

Transcription termination factor rho was purified to near homogeneity from the wild type and temperature-sensitive rho-111 mutant strains of Salmonella typhimurium. Each protein had identical physical properties with respect to native and subunit molecular weight, elution from ion-exchange columns, and poly(C)-dependent ATPase specific activity at 30 degrees C. The mutant protein exhibited a thermolabile poly(C)-dependent ATPase activity. The transcription termination and nascent RNA-dependent ATPase activities associated with the purified wild type S. typhimurium rho protein were not present in the mutant protein. Binding studies demonstrated that the stability of the rho-111:poly(C) complex was significantly more sensitive to ionic strength and temperature than that of the rho +: poly(C) complex. This result suggests that the altered activities of the mutant protein are due to its decreased ability to participate in a specific interaction with RNA which is insensitive to ionic strength. The rho-111 mutation resulted in a 20- to 30-fold elevation in the level of the mutant protein, indicating that rho biosynthesis in S. typhimurium is autogenously regulated. Therefore, defective molecular interactions between the mutant rho protein and RNA might account for the absence of transcription termination in vitro, and the polarity suppressor phenotype and defective autogenous regulation of rho biosynthesis in vivo.