Salmonella typhimurium mutants lacking ribonuclease I: effect on the polarity of histidine mutants.
Mutants of Salmonella typhimurium containing 1 to 2% of wild-type ribonuclease I activity were isolated. The rns mutation had no effect on the polarity of mutations in the S. typhimurium histidine operon. Even in the presence of an rns mutation, it was not possible to obtain strong suppressors of the polarity of two polar mutations in the his operon.
D000249:Adenosine Monophosphate / Q000096:biosynthesis; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D002474:Cell-Free System; D002855:Chromatography, Thin Layer; D000242:Cyclic AMP / Q000096:biosynthesis; D004492:Edetic Acid; D006639:Histidine / Q000096:biosynthesis*; D009153:Mutagens; D009154:Mutation; D009876:Operon; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011119:Polynucleotides / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012260:Ribonucleases / Q000096:biosynthesis* / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification; D013489:Suppression, Genetic
D009153:Mutagens; D011119:Polynucleotides; D000249:Adenosine Monophosphate; D006639:Histidine; D012343:RNA, Transfer; D004492:Edetic Acid; D000242:Cyclic AMP; D000429:Alcohol Oxidoreductases; D012260:Ribonucleases; D010744:Phosphoric Monoester Hydrolases