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Mono‐ADP‐Ribosylation of Arginine Residue of Euglena gracilis Z in Synchronous Culture
Author(s) -
TAKENAK SHIGEO,
INAGAKI JUNKO,
TSUYAMA SHINGO,
MIYATAKE KAZUTAKA,
NAKANO YOSHIHISA
Publication year - 1995
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1995.tb01596.x
Subject(s) - euglena gracilis , biology , euglena , arginine , chloroplast , biochemistry , organelle , cytosol , mitochondrion , enzyme , microsome , residue (chemistry) , microbiology and biotechnology , amino acid , gene
. 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 marker enzyme activities and the activity in each organelle fluctuated with the cell cycle.