Open AccessDifferential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction
Author(s) -
Onda Yayoi,
Kobori Yohei
Publication year - 2014
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2014.07.007
Subject(s) - protein disulfide isomerase , disulfide bond , chemistry , biochemistry , reduction (mathematics) , geometry , mathematics
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.