Glutamine synthetase of Chlamydomonas: Rapid reversible deactivation.

A 70% reduction in glutamine synthetase (GS) activity was observed within 5 min when 5 mM NH3 and darkness was applied to steady-state cells of Chlamydomonas utilising NO3. The enzyme was reactivated in vivo by reillumination of the culture and in vitro by treatment with thiol reagents. The activity modulations affected the synthetase and transferase activities similarly and were not influenced by protein synthesis inhibitors. Deactivation of GS was also observed when steady-state cells were treated with an uncoupler of phosphorylation, carbonylcyanide m-chlorophenylhydrazone (CCCP) or inhibitors of the electron transport chain but under these conditions the activity modulation affected over 90% of the activity and was irreversible. The mechanism of the physiological deactivation of GS is discussed in relation to both the in vivo and in vitro findings.