Abstract
The redox state of glutathione, which is the most abundant tripeptide thiol in the living cell, changes with environmental stress. We considered that protein glutathionylation may be the key step in the cellular perception of changes in redox environments. We succeeded in identification of glutathionylated proteins using biotinated glutathione in the Arabidopsis suspension-cultured cells [Ito et al. (2003) Plant Cell Physiol. 44: 655]. One of the glutathionylated proteins proved translationally controlled tumor protein like protein (TCTP), which has been believed to be involved in the division of vertebrate cells. Recombinant TCTP was also in vitro glutathionylated in the presence of oxidized glutathione. Now we are investigating the function of this protein.
