Nitrogen Regulation of Glutamine Synthetase in Neurospora crassa

Abstract

A higher activity of glutamine synthetase (EC 6.3.1.2] was found in N. crassa when NH4+ was limiting as N source than when glutamate was limiting. When glutamate, glutamine or NH4+ were in excess, a lower activity was found. Immunological titration and sucrose gradient sedimentation of the enzyme established that under all these conditions enzyme activity corresponded to enzyme concentration and that the octamer was the predominant oligomeric form. When N. crassa was shifted from N-limiting substrates to excess product as N source, the concentration of glutamine synthetase was adjusted with kinetics that closely followed dilution by growth. When grown on limiting amounts of glutamate, a lower oligomer was present in addition to the octameric form of the enzyme. When the culture was shifted to excess NH4+, glutamine accumulated at a high rate; nevertheless, there was only a slow decrease in enzyme activity and no modification of the oligomeric pattern.