title: Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction.
abstract: 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.
authors.affiliation: Department of Food and Applied Life Sciences, Yamagata University, 1-23 Wakaba-Machi, Tsuruoka, Yamagata 997-8555, Japan.
authors.forename: Yayoi
authors.initials: Y
authors.lastname: Onda
authors.affiliation: Department of Food and Applied Life Sciences, Yamagata University, 1-23 Wakaba-Machi, Tsuruoka, Yamagata 997-8555, Japan.
authors.forename: Yohei
authors.initials: Y
authors.lastname: Kobori
keywords: Disulfide bond; ER, endoplasmic reticulum; ERO1, ER oxidoreductin 1; GSH, glutathione; GSSG, glutathione disulfide; Glutathione; PDI; PDI, protein disulfide isomerase; Protein storage organelle; Rice; TRX, thioredoxin