Os09g0451500

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Annotated Information

Function

Protein disulfide isomerase (PDI), a ubiquitous sulfhydryl oxidoreductase found in all eukaryotic cells, is multifunctional enzyme, which catalyzes a wide range of thiol-disulfide exchange reactions, including oxidation, reduction, and isomerization, and also displays chaperone activity. PDIL2;3 and PDIL1;1 are not functionally redundant in sulfhydryl oxidations of structurally diverse storage proteins and play distinct roles in PB development. PDIL2;3-dependent and PDIL2;3-independent oxidation pathways that sustain disulfide bonds of crP10 in PB-I.

Expression

Complementation analyses using PDIL1;1 knockout esp2 mutant indicated that the a and a' TRX domains of PDIL1;1 exhibited similar redox activities and that PDIL2;3 was unable to perform the PDIL1;1 functions. PDIL2;3 knockdown inhibited the accumulation of Cys-rich 10-kD prolamin (crP10) in the core of PB-I. Conversely, crP10 knockdown dispersed PDIL2;3 into the ER lumen. Glutathione S-transferase-PDIL2;3 formed a stable tetramer when it was expressed in Escherichia coli, and the recombinant PDIL2;3 tetramer facilitated α-globulin(C79F) mutant protein to form nonnative intermolecular disulfide bonds in vitro.

Evolution

Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen.

Labs working on this gene

Division of Plant Sciences, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan

Institute of Genetic Resources, Faculty of Agriculture, Kyushu University, Hakozaki, Fukuoka 812-8581, Japan

Faculty of Life Science, Yamaguchi Prefectural University, Sakurabatake, Yamaguchi 753-8502, Japan

References

Yayoi Onda;Ai Nagamine;Mutsumi Sakurai;Toshihiro Kumamaru;Masahiro Ogawa;Yasushi Kawagoe Distinct Roles of Protein Disulfide Isomerase and P5 Sulfhydryl Oxidoreductases in Multiple Pathways for Oxidation of Structurally Diverse Storage Proteins in Rice The Plant Cell, 2011, 23(1): 210-223