General control of arginine biosynthetic enzymes in Neurospora crassa

Abstract

The response of six amino acid synthetic enzymes, including four concerned with arginine synthesis, one with histidine synthesis and one with lysine synthesis, to conditions of histidine and arginine limitation and to exogenously provided amino acids is described in Neurospora crassa. The activities of all these enzymes increased in response to lowered levels of histidine or arginine, but showed little or no repression in wild-type cultures supplemented with casein hydrolysate. The activity of glucose-6-phosphate dehydrogenase (an enzyme not concerned with amino acid synthesis) remained unaffected by any of these conditions. In the case of the four arginine synthetic enzymes evidence is presented that suggests the "general' system implicated in the 'cross-pathway' response to histidine is also entirely responsible for the derepression occurring under conditions of arginine limitation. Further investigations into the control of one enzyme, ornithine carbamoyltransferase, are also reported. These show that the enzyme is stable, and suggest that its derepression in response to histidine limitation entails new protein synthesis and involves control at a stage prior to translation.