Regeneration of invertase in Neurospora crassa.

In Neurospora, invertase is predominately an extracellular enzyme, and acid phosphatase is partially external in location. Both extracellular invertase and acid phosphatase were rapidly and quantitatively inactivated by acid treatment (pH 1.3). When such acid-treated cells were incubated with a suitable carbon source, a substantial regeneration of invertase activity occurred, but no restoration of acid phosphatase could be detected. The regeneration of invertase does not occur by renaturation of the inactivated enzyme, nor by secretion of a preexisting intracellular pool of invertase, but instead requires de novo enzyme synthesis. Invertase synthesis was partially repressed by glucose and mannose and was completely inhibited by 2-deoxyglucose. Acetate was found to inhibit invertase regeneration and the transport and incorporation of uracil and leucine. Several potential inhibitors of transcription, including alpha-amanitin, 5-fluorouracil, actinomycin D, and three derivatives of rifamycin, were ineffective in preventing invertase regeneration and in inhibiting the synthesis of ribonucleic acid. Conidia appeared to be very poorly permeable to these compounds.