Mono‐ADP‐Ribosylation of Arginine Residue of Euglena gracilis Z in Synchronous Culture

SHIGEO TAKENAK, JUNKO INAGAKI, SHINGO TSUYAMA, KAZUTAKA MIYATAKE, YOSHIHISA NAKANO

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

ABSTRACT. 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.

Original languageEnglish
Pages (from-to)373-376
Number of pages4
JournalJournal of Eukaryotic Microbiology
Volume42
Issue number4
DOIs
Publication statusPublished - Jul 1995

Keywords

  • Cell cycle
  • Euglena gracilis Z
  • NAD
  • cytokinesis
  • organelles organellogenesis

ASJC Scopus subject areas

  • Microbiology

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