Acetylglucosaminidase, an early enzyme in the development of Dictyostelium discoideum

Abstract

The specific activity of acetylglucosaminidase has been found to increase more than 10-fold during the first 10 hr of development in the cellular slime mold Dictyostelium discoideum. The specific activity then remained essentially constant until after germination. The activity was purified 36-fold and found to behave as a single protein species. The increase in specific activity required concomitant protein synthesis. If ribonucleic acid synthesis was preferentially inhibited during the period of synthesis of acetylglucosaminidase, further increase in enzymatic activity stopped after 2 hr. The increase in activity did not occur in a mutant strain which did not undergo the first step in morphogenesis. Mutant strains, blocked slightly later in morphogenesis, synthesized the enzyme at the normal rate but for an extended period. It was concluded that the initiation and termination of synthesis of acetylglucosaminidase are controlled by the developmental program.