MONO-ADP-RIBOSYLATION OF ARGININE RESIDUE OF EUGLENA-GRACILIS-Z IN SYNCHRONOUS CULTURE

In Euglena gracilis Z, a considerably high activity of mono-ADP-ribosy ltransferase occurred and change of it was accompanied by a cell cycle induced by a light-dark cycle. The enzyme activity was strongly inhib ited by L-arginine and supported in the presence of poly-L-arginine as a substrate, indicating that ADP-ribosylated amino acid is an arginin e residue. Arginine: mono-ADP-ribosyltransferase activity was found in the chloroplasts, mitochondria, microsomes and cytosol as judged from marker enzyme activities and the activity in each organelle fluctuate d with the cell cycle.