Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice.

@article{Onda2011DistinctRO,
  title={Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice.},
  author={Yayoi Onda and Ai Nagamine and Mutsumi Sakurai and Toshihiro Kumamaru and Masahiro Ogawa and Yasushi Kawagoe},
  journal={The Plant cell},
  year={2011},
  volume={23 1},
  pages={210-23}
}
In the rice (Oryza sativa) endosperm, storage proteins are synthesized on the rough endoplasmic reticulum (ER), in which prolamins are sorted to protein bodies (PBs) called type-I PB (PB-I). 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… CONTINUE READING
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Isolation and characterization of 2-types of protein bodies in the rice endosperm

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  • Agric. Biol. Chem
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