Defective guanine uptake in an 8-azaguanine-resistant mutant of Salmonella typhimurium.

An 8-azaguanine-resistant mutant, azg-11, derived from a guanine auxotroph, gua-1, of Salmonella typhimurium was isolated. This mutant was resistant to the analogue when grown on 2,6-diaminopurine, but showed greater susceptibility than the parent on guanine. Studies with the uptake of radioactive purines revealed that the mutant was defective in a mechanism for incorporation of guanine as well as of xanthine. Initial rates of uptake were determined for guanine at concentrations which were sufficiently low to make permeases limiting. The affinity constant K(m) for the mutant was found to be 2.5 x 10(-4)m; that of the parent was 2.3 x 10(-5)m. Examination of cell-free extracts suggested that the purine nucleotide pyrophosphorylases, responsible for the conversion of free intracellular purines to the corresponding nucleotides, were present and unaltered. The results indicate that the mutant is defective in a mechanism for the active transport for guanine and possibly xanthine.