First enzyme of histidine biosynthesis and repression control of histidyl-transfer ribonucleic acid synthetase of Salmonella typhimurium.
The regulation of formation of histidyl-transfer ribonucleic acid (tRNA) synthetase was examined in strains of Salmonella typhimurium. When the first of the histidine-forming enzymes was wild type, the presence of 2-thiazolealanine in the growth medium prevented repression of histidyl-tRNA synthetase formation elicited by the addition of 1, 2, 4-triazole-3-alanine to these cultures. Conversely, thiazolealanine had no effect on repression of histidyl-tRNA synthetase formation by triazolealanine in hisG mutant strains. These data suggest a relationship between the control of histidyl-tRNA synthetase formation and the functional state of the histidine operon.
D000596:Amino Acids / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000096:biosynthesis*; D002250:Carbon Radioisotopes; D002474:Cell-Free System; D004794:Enzyme Repression / Q000187:drug effects; D006639:Histidine / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000494:pharmacology; D007930:Leucine; D009154:Mutation; D009876:Operon; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000378:metabolism; D013844:Thiazoles; D014230:Triazoles
D000596:Amino Acids; D002250:Carbon Radioisotopes; D013844:Thiazoles; D014230:Triazoles; D006639:Histidine; D000604:Amino Acyl-tRNA Synthetases; D007930:Leucine