Abstract
Cellular levels of an L-asparaginase in a Chlamydomonas species were found to be greater in nitrogen-limited batch cultures than in batch cultures grown in ample nitrogen. Cells grown in high nitrogen medium (5 mM NH4Cl) and suspended in nitrogen-free medium showed a 2- to 3.5-fold increase in activity after 24 to 48 h. This increase in activity was inhibited by cycloheximide and by the addition of high levels of combined nitrogen (5 mM NH4Cl, NaNO3, or L-asparagine), suggesting repression by ambient nitrogen levels as the mode of regulation of this enzyme. Derepressed L-asparaginase activity did not disappear in the presence of high concentrations of medium nitrogen, indicating the absence of an asparaginase-degrading system. Derepression of asparaginase by this organism was light dependent and inhibited by 3-(3',4'-dichlorophenyl)-1,1-dimethylurea suggesting a requirement for photosynthetic energy.