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The World of Protozoa, Rotifera, Nematoda and Oligochaeta

Ref ID : 7351

Takenaka Shigeo, Inagaki Junko, Tsuyama Shingo, Miyatake Kazutaka, and Nakano Yoshihisa; Mono-ADP-Ribosylation of Arginine Residue of Euglena gracilis Z in Synchronous Culture. J.Eukaryot.Microbiol. 42(4):373-376, 1995

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