Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

• PDIL1;1 efficiently catalyzed both disulfide bond formation and disulfide bond reduction.
• Two redox-active sites of PDIL1;1 were involved in disulfide reduction.
• Disulfide reduction activity of PDIL1;1 increased with increasing GSH concentration.

Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1, PDIL1;4, and PDIL2;3) and found that PDIL1;1 exhibited the highest catalytic activity for both disulfide bond formation and disulfide bond reduction. The activity of PDIL1;1-catalyzed disulfide bond reduction, in which two redox-active sites were involved, was enhanced by increasing the glutathione concentration. These results suggest that PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging.