| Abstract: | Gastrula-stage embryos of the brine shrimp Artemia undergo reversible transitions between metabolically active and dormant states that are promoted by changes in intracellular pH. A macromolecular mechanism for this suppression of energy metabolism that involves regulation of the enzyme trehalase is reported here. Isolated trehalase from these embryos existed in two active forms that interconverted when exposed to physiological transitions in pH. This hysteretic interconversion was reversible, required minutes for completion, and involved a change in enzyme polymerization. The two states differed twofold in molecular size and were distinguishable electrophoretically. Compared to the smaller species, the polymerized form was strongly inhibited by acidic pH, adenosine 5'-triphosphate, and the substrate trehalose. Thus, the shift in assembly equilibrium toward the aggregated enzyme caused by pH values less than or equal to 7.4 may mediate the arrest of trehalose-fueled metabolism and respiration during dormancy in this cryptobiotic organism. |
