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Salmonella typhimurium Mutants Lacking Ribonuclease I: Effect on the Polarity of Histidine Mutants

^a Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014

ABSTRACT

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.

¹ Present address: Istituto di Patologia Generale, Università di Napoli, Naples, Italy.

² Present address: Clinical Endocrinology Branch, National Institute of Arthritis, Metabolism, and Digestive Diseases, Bethesda, Md. 20014.