Redox regulation of glutenin subunit assembly in the plant endoplasmic reticulum

The glutenin fraction of wheat storage proteins consists of large polymers in which high- and low-molecular-weight subunits are connected by interchain disulfide bonds. We find that the assembly of a low-molecular-weight glutenin subunit in the endoplasmic reticulum is a rapid process that leads to the accumulation of a set of different oligomeric forms, and that this assembly is sensitive to perturbation of the cellular redox environment. In endoplasmic reticulum-derived microsomes, low-molecular-weight glutenin subunits are subjected to hyperpolymerization, indicating that cytosolic factors play an important role in limiting polymer size. Addition of physiological concentrations of reduced glutathione are sufficient to maintain the original polymerization pattern of the glutenin subunits upon cytosol dilution. Furthermore, we show that a low-molecular-weight glutenin subunit can be glutathionylated in endoplasmic reticulum-derived microsomes, and that it can be directly reduced by glutathione in vitro. These results indicate that glutenin polymerization is sensitive to changes in the redox state of the cell, and suggest that the presence of a reducing cytosolic environment plays an important role in regulating disulfide bond formation in the endoplasmic reticulum of plant cells.