Genetic studies of mutants in a high-affinity methionine transport system in Salmonella typhimurium.

A total of 30 metP mutations defective in the high-affinity methionine transport system were linked in P1 transduction to the zaf-1351::Tn10 insertion mutation at min 5-6 on the Salmonella typhimurium chromosome map. The relationship of metP to several other markers in this region was studied. Methionine transport was strongly inhibited by arsenate, suggesting that the metP system belongs to the shock-sensitive category and possesses a periplasmic binding protein. However, other experiments provided less clear cut evidence. Transport activity was only slightly reduced by osmotic shock; a methionine binding activity was detected in shock fluids from the wild-type strain, and although this activity was reduced by 50% in 3 frameshift mutants, mutants without any activity were not found. No differences were detected in the shock fluids of the 30 mutants when examined by SDS-polyacrylamide gel electrophoresis.