Histidine-mediated control of tryptophan biosynthetic enzymes in Neurospora crassa.
The formation of the five tryptophan biosynthetic enzymes of Neurospora crassa was shown to be derepressed in histidine-starved cells. This histidine-mediated derepression was not due to a lowered intracellular concentration of tryptophan in these cells. Furthermore, histidine-mediated derepression of tryptophan enzymes was found to be coordinate and not subject to reversal by tryptophan of either exogenous or biosynthetic origin. The synthesis of tryptophan enzymes also was found to be coordinate in cells which were not histidine-starved. Although histidine is clearly involved in regulating the synthesis of tryptophan enzymes, it did not prevent either tryptophan-mediated derepression of tryptophan enzymes or indole-3-glycerol phosphate-mediated derepression of tryptophan synthetase.
D006639:Histidine / Q000378:metabolism*; D007211:Indoles / Q000378:metabolism; D007535:Isomerases / Q000096:biosynthesis; D008025:Ligases / Q000096:biosynthesis*; D009154:Mutation; D009491:Neurospora / Q000201:enzymology*; D014166:Transferases / Q000096:biosynthesis*; D014364:Tryptophan / Q000378:metabolism*
D007211:Indoles; D006639:Histidine; D014364:Tryptophan; D014166:Transferases; D007535:Isomerases; D008025:Ligases