Abstract
Reactive oxygen species (ROS) are produced in plant cells under various stress conditions and are also generated in the defense responses against pathogen attacks and believed to act as the signal molecules. But the perception mechanism of ROS is not fully understood. We considered that the glutathionylation of proteins that is mediated by ROS is the key step in the perception of ROS. We tried to identify the glutathionylated proteins using biotinated glutathione.
Biotinated glutathione was obtained by reacting biotinamidocaproic acid 3-sulfo-N-hydroxysuccinimide with glutathione. After incubation of the Arabidopsis suspension cells with biotinated glutathione, some glutathionylated proteins were detected by the biotin tag. This indicates the incorporation of glutathione to proteins in the cell.
One of them proved triose-phosphate isomerase. The activity of recombinant protein was modulated by glutathione, suggesting that the activity of triose-phosphate isomerase would be regulated by glutathione redox status of the cell.
