Induction potential for glyoxylate cycle enzymes during the cell cycle of Euglena gracilis.
In light/dark synchronized cultures of Euglena gracilis Klebs Z the enzymes malate synthase, isocitrate lyase and acetate thiokinase were induced upon addition of acetate at all stages of the cell cycle. Cycloheximide and p-fluorophenylalanine inhibited the development of enzyme activity, showing that induction was dependent on protein synthesis. The maximum rate of induction for all three enzymes was constant for much of the cell cycle but doubles in a single step during the period of DNA replication. Although these data indicate that enzyme potential was regulated by gene dosage and that the structural gene for each enzyme was continuously available for transcription during the cell-cycle it was not possible by using inhibitors of RNA synthesis, to demonstrate concurrent transcription during enzyme induction.
D000106:Acetate-CoA Ligase / Q000378:metabolism; D000818:Animals; D002455:Cell Division / Q000187:drug effects; D003513:Cycloheximide / Q000494:pharmacology; D005056:Euglena gracilis / Q000187:drug effects / Q000201:enzymology*; D006038:Glyoxylates / Q000378:metabolism*; D007523:Isocitrates; D007700:Kinetics; D008293:Malates; D007652:Oxo-Acid-Lyases / Q000378:metabolism; D013997:Time Factors; D010135:p-Fluorophenylalanine / Q000494:pharmacology
D006038:Glyoxylates; D007523:Isocitrates; D008293:Malates; D010135:p-Fluorophenylalanine; D003513:Cycloheximide; D007652:Oxo-Acid-Lyases; D000106:Acetate-CoA Ligase