New methionine structural gene in Salmonella typhimurium.
Eight metH mutants in Salmonella typhimurium with closely linked sites of mutation which could grow only on methionine were isolated from a metE mutant deficient in N(5)-methyltetrahydropteroyltriglutamate-homocysteine transmethylase; their deficiency in cobalamin-dependent N(5)-methyltetrahydrofolate-homocysteine transmethylase was supported by the results of enzyme studies of one of them. Cotransduction of metH and metA (homoserine O-transsuccinylase) mutants was obtained, thus revealing linkage between a second pair of the six known methionine structural genes. One metH mutant clearly differed from the rest in that it reverted at a higher frequency, was temperature sensitive, complemented all other metH mutants, and was located farthest from the metA gene.
D002874:Chromosome Mapping; D005827:Genetics, Microbial; D006710:Homocysteine / Q000378:metabolism; D008715:Methionine / Q000378:metabolism*; D008745:Methylation; D008967:Molecular Biology; D009154:Mutation; D012486:Salmonella typhimurium / Q000201:enzymology / Q000378:metabolism*; D013696:Temperature; D014161:Transduction, Genetic
D006710:Homocysteine; D008715:Methionine