Abstract
Thioredoxin (Trx) is a small ubiquitous protein that regulates a number of phenomena via formation or reduction of a disulphide bridge in the target enzyme. Cytosolic thioredoxin has been reported to regulate several membrane proteins that involve in the self-incompatibility and in the innate immunity of plant so far.
To elucidate target proteins of cytosolic thioredoxin in plant membranes comprehensively, we prepared a plasma membrane-enriched fraction from the suspension culture of Arabidopsis thaliana, and solubilized proteins were subjected to the thioredoxin affinity chromatography method. The captured proteins were identified by MALDI-TOF/TOF MS analysis. We present a list of potential targets for thioredoxin including the proteins, which function for the signal transduction. We here discuss the physiological meaning of the redox regulation of the membrane signaling molecules in plant cells based on the results of our thioredoxin affinity chromatography.
